RPOC_ECOLI
ID RPOC_ECOLI Reviewed; 1407 AA.
AC P0A8T7; P00577; P00578; P78134; Q2M8S4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
GN Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322}; Synonyms=tabB;
GN OrderedLocusNames=b3988, JW3951;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-8, AND PARTIAL
RP PROTEIN SEQUENCE.
RX PubMed=6287430; DOI=10.1093/nar/10.13.4035;
RA Ovchinnikov Y.A., Monastyrskaya G.S., Gubanov V.V., Guryev S.O.,
RA Salomatina I.S., Shuvaeva T.M., Lipkin V.M., Sverdlov E.D.;
RT "The primary structure of E. coli RNA polymerase, Nucleotide sequence of
RT the rpoC gene and amino acid sequence of the beta'-subunit.";
RL Nucleic Acids Res. 10:4035-4044(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-176.
RA Monastyrskaya G.S., Gubanov V.V., Guryev S.O., Lipkin V.M., Sverdlov E.D.;
RT "Primary structure of EcoRI-F fragment of rpoB, C genes and corresponding
RT fragments of beta- and beta'-subunits of RNA polymerase from E.coli.";
RL Bioorg. Khim. 6:1106-1109(1980).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-176.
RA Gurevich A.I., Igoshin A.V., Kolosov M.N.;
RT "Structure of a central part of E.coli operon rpoBC. Nucleotide sequence of
RT the gene for beta subunit of RNA polymerase.";
RL Bioorg. Khim. 6:1580-1584(1980).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-176, AND PROTEIN SEQUENCE OF 1-8.
RX PubMed=6266829; DOI=10.1111/j.1432-1033.1981.tb05381.x;
RA Ovchinnikov Y.A., Monastyrskaya G.S., Gubanov V.V., Guryev S.O.,
RA Chertov O.Y., Modyanov N.N., Grinkevich V.A., Makarova I.A.,
RA Marchenko T.V., Polovnikova I.N., Lipkin V.M., Sverdlov E.D.;
RT "The primary structure of Escherichia coli RNA polymerase. Nucleotide
RT sequence of the rpoB gene and amino-acid sequence of the beta-subunit.";
RL Eur. J. Biochem. 116:621-629(1981).
RN [8]
RP PROTEIN SEQUENCE OF 1-4.
RC STRAIN=K12;
RX PubMed=1095419; DOI=10.1016/0014-5793(75)81001-5;
RA Fujiki H., Zurek G.;
RT "The subunits of DNA-dependent RNA polymerase from E. coli: I. Amino acid
RT analysis and primary structure of the N-terminal regions.";
RL FEBS Lett. 55:242-244(1975).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 175-988.
RA Monastyrskaya G.S., Guryev S.O., Kalinina N.F., Sorokin A.V.,
RA Salomatina I.S., Shuvaeva T.M., Lipkin V.M., Sverdlov E.D.,
RA Ovchinnikov Y.A.;
RT "Primary structure of EcoRI-D fragment of rpoC gene and corresponding
RT fragment of beta-subunit of RNA polymerase from E.coli.";
RL Bioorg. Khim. 8:130-134(1982).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 987-1407.
RA Ovchinnikov Y.A., Monastyrskaya G.S., Gubanov V.V., Salomatina I.S.,
RA Shuvaeva T.M., Lipkin V.M., Sverdlov E.D.;
RT "Primary structure of RNA polymerase from E.coli. Nucleotide sequence of
RT E.coli DNA fragment containing a part of the rpoC gene and the
RT corresponding C-terminal amino acid sequence of beta'-subunit.";
RL Bioorg. Khim. 7:1107-1112(1981).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1073-1407.
RC STRAIN=K12;
RX PubMed=6278450; DOI=10.1093/nar/9.24.6827;
RA Squires C., Krainer A., Barry G., Shen W.-F., Squires C.L.;
RT "Nucleotide sequence at the end of the gene for the RNA polymerase beta'
RT subunit (rpoC).";
RL Nucleic Acids Res. 9:6827-6840(1981).
RN [12]
RP FUNCTION IN TRANSCRIPTION, AND SUBUNIT.
RX PubMed=1646077; DOI=10.1016/0092-8674(91)90553-b;
RA Igarashi K., Ishihama A.;
RT "Bipartite functional map of the E. coli RNA polymerase alpha subunit:
RT involvement of the C-terminal region in transcription activation by cAMP-
RT CRP.";
RL Cell 65:1015-1022(1991).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-983, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [14]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [15]
RP ACETYLATION.
RX PubMed=21696463; DOI=10.1111/j.1365-2958.2011.07742.x;
RA Lima B.P., Antelmann H., Gronau K., Chi B.K., Becher D., Brinsmade S.R.,
RA Wolfe A.J.;
RT "Involvement of protein acetylation in glucose-induced transcription of a
RT stress-responsive promoter.";
RL Mol. Microbiol. 81:1190-1204(2011).
RN [16] {ECO:0007744|PDB:3IYD}
RP STRUCTURE BY ELECTRON MICROSCOPY (19.80 ANGSTROMS) IN COMPLEX WITH RPOA;
RP RPOB; RPOD; RPOZ; CRP AND DNA, DNA-BINDING, AND SUBUNIT.
RX PubMed=19903881; DOI=10.1073/pnas.0908782106;
RA Hudson B.P., Quispe J., Lara-Gonzalez S., Kim Y., Berman H.M., Arnold E.,
RA Ebright R.H., Lawson C.L.;
RT "Three-dimensional EM structure of an intact activator-dependent
RT transcription initiation complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19830-19835(2009).
RN [17] {ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY}
RP X-RAY CRYSTALLOGRAPHY (3.90 ANGSTROMS) IN COMPLEX WITH RPOA; RPOB; RPOD;
RP RPOZ; SALINAMIDE A; MAGNESIUM AND ZINC, FUNCTION, COFACTOR, SUBUNIT,
RP BIOTECHNOLOGY, ANTIBIOTIC RESISTANCE, AND MUTAGENESIS OF GLN-504; ASN-690;
RP MET-697; ALA-735; ARG-738; ALA-748; PRO-758; PHE-763; SER-775; ALA-779;
RP ARG-780; GLY-782 AND LEU-783.
RX PubMed=24843001; DOI=10.7554/elife.02451;
RA Degen D., Feng Y., Zhang Y., Ebright K.Y., Ebright Y.W., Gigliotti M.,
RA Vahedian-Movahed H., Mandal S., Talaue M., Connell N., Arnold E.,
RA Fenical W., Ebright R.H.;
RT "Transcription inhibition by the depsipeptide antibiotic salinamide A.";
RL Elife 3:e02451-e02451(2014).
RN [18] {ECO:0007744|PDB:6TQN, ECO:0007744|PDB:6TQO}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF RRNA
RP TRANSCRIPTION-ELONGATION-ANTITERMINATION COMPLEXES WITH AND WITHOUT S4 IN
RP COMPLEX WITH MAGNESIUM AND ZINC, FUNCTION, SUBUNIT, AND COFACTOR.
RX PubMed=32871103; DOI=10.1016/j.molcel.2020.08.010;
RA Huang Y.H., Hilal T., Loll B., Buerger J., Mielke T., Boettcher C.,
RA Said N., Wahl M.C.;
RT "Structure-Based Mechanisms of a Molecular RNA Polymerase/Chaperone Machine
RT Required for Ribosome Biosynthesis.";
RL Mol. Cell 0:0-0(2020).
CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC transcription of DNA into RNA using the four ribonucleoside
CC triphosphates as substrates. {ECO:0000255|HAMAP-Rule:MF_01322,
CC ECO:0000269|PubMed:1646077, ECO:0000269|PubMed:24843001}.
CC -!- FUNCTION: Resistance to the antibiotics salinamide A, salinamide B,
CC rifampicin, streptolydigin, CBR703, myxopyronin, and lipiarmycin can
CC result from mutations in this protein. {ECO:0000269|PubMed:24843001,
CC ECO:0000305|PubMed:24843001}.
CC -!- FUNCTION: Part of the processive rRNA transcription and antitermination
CC complex (rrnTAC). The complex forms an RNA-chaperone ring around the
CC RNA exit tunnel of RNAP. It supports rapid transcription and
CC antitermination of rRNA operons, cotranscriptional rRNA folding, and
CC annealing of distal rRNA regions to allow correct ribosome biogenesis.
CC {ECO:0000269|PubMed:32871103}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:24843001, ECO:0000269|PubMed:32871103,
CC ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:24843001,
CC ECO:0000269|PubMed:32871103, ECO:0007744|PDB:4MEX,
CC ECO:0007744|PDB:4MEY};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:24843001, ECO:0000269|PubMed:32871103,
CC ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:24843001,
CC ECO:0000269|PubMed:32871103};
CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC and 1 omega subunit. When a sigma factor is associated with the core
CC the holoenzyme is formed, which can initiate transcription. The rRNA
CC transcription and antitermination complex (rrnTAC) consists of RNAP,
CC NusA, NusB, NusE (rpsJ), NusG, SubB, ribosomal protein S4, DNA and
CC precursor rRNA; S4 is more flexible than other subunits
CC (PubMed:32871103). {ECO:0000255|HAMAP-Rule:MF_01322,
CC ECO:0000269|PubMed:1646077, ECO:0000269|PubMed:19903881,
CC ECO:0000269|PubMed:24843001, ECO:0000269|PubMed:32871103}.
CC -!- INTERACTION:
CC P0A8T7; P69441: adk; NbExp=2; IntAct=EBI-543604, EBI-543592;
CC P0A8T7; P0A6Z3: htpG; NbExp=3; IntAct=EBI-543604, EBI-369221;
CC P0A8T7; P0A8V2: rpoB; NbExp=11; IntAct=EBI-543604, EBI-544996;
CC P0A8T7; P00579: rpoD; NbExp=11; IntAct=EBI-543604, EBI-545104;
CC P0A8T7; P03018: uvrD; NbExp=3; IntAct=EBI-543604, EBI-559573;
CC -!- PTM: Acetylated on several lysine residues in the presence of glucose.
CC {ECO:0000269|PubMed:18723842, ECO:0000269|PubMed:21696463}.
CC -!- BIOTECHNOLOGY: Co-administration of salinamide and rifampicin or
CC salinamide and myxopyronin suppresses the emergence of resistance to
CC both antibiotics. {ECO:0000269|PubMed:24843001}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
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DR EMBL; V00339; CAA23626.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43086.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76962.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77332.1; -; Genomic_DNA.
DR EMBL; M38293; AAA24582.1; -; Genomic_DNA.
DR EMBL; M38303; AAA24584.1; -; Genomic_DNA.
DR EMBL; V00340; CAA23628.1; -; Genomic_DNA.
DR EMBL; M38305; AAA24586.1; -; Genomic_DNA.
DR EMBL; M38288; AAA24408.1; -; Genomic_DNA.
DR PIR; A00695; RNECC.
DR RefSeq; NP_418415.1; NC_000913.3.
DR RefSeq; WP_000653944.1; NZ_STEB01000045.1.
DR PDB; 2AUK; X-ray; 2.30 A; A/B/C/D/E=944-1129.
DR PDB; 2LMC; NMR; -; B=1151-1213.
DR PDB; 3IYD; EM; -; D=1-1407.
DR PDB; 3LU0; EM; -; D=1-1407.
DR PDB; 4IQZ; X-ray; 2.10 A; A/B/C/D/E=932-1141.
DR PDB; 4JK1; X-ray; 3.90 A; D/I=1-1407.
DR PDB; 4JK2; X-ray; 4.20 A; D/I=1-1407.
DR PDB; 4KMU; X-ray; 3.85 A; D/I=1-1407.
DR PDB; 4KN4; X-ray; 3.96 A; D/I=1-1407.
DR PDB; 4KN7; X-ray; 3.69 A; D/I=1-1407.
DR PDB; 4MEX; X-ray; 3.90 A; D/J=1-1407.
DR PDB; 4MEY; X-ray; 3.95 A; D/J=1-1407.
DR PDB; 4XSX; X-ray; 3.71 A; D/J=1-1407.
DR PDB; 4XSY; X-ray; 4.01 A; D/J=1-1407.
DR PDB; 4XSZ; X-ray; 3.68 A; D/J=1-1407.
DR PDB; 4YG2; X-ray; 3.70 A; D/J=1-1407.
DR PDB; 4YLN; X-ray; 5.50 A; D/J/P=1-1407.
DR PDB; 4YLO; X-ray; 6.00 A; D/J/P=1-1407.
DR PDB; 4YLP; X-ray; 5.50 A; D/J/P=1-1407.
DR PDB; 4ZH2; X-ray; 4.20 A; D/J=1-1407.
DR PDB; 4ZH3; X-ray; 4.08 A; D/J=1-1407.
DR PDB; 4ZH4; X-ray; 3.99 A; D/J=1-1407.
DR PDB; 5BYH; X-ray; 3.76 A; D=1-1407.
DR PDB; 5EZK; X-ray; 8.50 A; D=1-1407.
DR PDB; 5IPL; X-ray; 3.60 A; D=1-1407.
DR PDB; 5IPM; X-ray; 4.20 A; D=1-1407.
DR PDB; 5IPN; X-ray; 4.61 A; D=1-1407.
DR PDB; 5MS0; EM; 9.80 A; D=1-1407.
DR PDB; 5MY1; EM; 7.60 A; Y=1-1407.
DR PDB; 5NSR; EM; 3.80 A; D=1-1407.
DR PDB; 5NSS; EM; 5.80 A; D=1-1407.
DR PDB; 5NWT; X-ray; 3.76 A; D=1-1407.
DR PDB; 5UAC; X-ray; 3.80 A; D/J=1-1407.
DR PDB; 5UAG; X-ray; 3.40 A; D/J=1-1407.
DR PDB; 5UAH; X-ray; 4.10 A; D/J=1-1407.
DR PDB; 5UAJ; X-ray; 3.92 A; D/J=1-1407.
DR PDB; 5UAL; X-ray; 3.89 A; D/J=1-1407.
DR PDB; 5UAQ; X-ray; 3.60 A; D/J=1-1407.
DR PDB; 5VSW; X-ray; 4.29 A; D/J=1-1407.
DR PDB; 5VT0; EM; 3.78 A; J=1-1407.
DR PDB; 5W1S; X-ray; 3.81 A; D/J=1-1407.
DR PDB; 5W1T; X-ray; 4.50 A; D/J=1-1407.
DR PDB; 6ALF; EM; 4.10 A; J=1-1407.
DR PDB; 6ALG; EM; 3.70 A; J=1-1407.
DR PDB; 6ALH; EM; 4.40 A; J=1-1407.
DR PDB; 6ASX; EM; 3.80 A; J=1-1407.
DR PDB; 6BJS; EM; 5.50 A; J=1-1407.
DR PDB; 6BYU; X-ray; 3.60 A; D/J=1-1407.
DR PDB; 6C6S; EM; 3.70 A; J=1-1407.
DR PDB; 6C6T; EM; 3.50 A; J=1-1407.
DR PDB; 6C6U; EM; 3.70 A; J=1-1407.
DR PDB; 6C9Y; EM; 4.25 A; D=1-1407.
DR PDB; 6CA0; EM; 5.75 A; D=1-1407.
DR PDB; 6CUX; X-ray; 4.10 A; D/J=1-1407.
DR PDB; 6FLP; EM; 4.10 A; D=1-1407.
DR PDB; 6FLQ; EM; 4.10 A; D=1-1407.
DR PDB; 6GFW; EM; 3.70 A; D=1-1407.
DR PDB; 6GH5; EM; 3.40 A; D=1-1407.
DR PDB; 6GH6; EM; 4.10 A; D=1-1407.
DR PDB; 6JBQ; EM; 4.02 A; D=1-1407.
DR PDB; 6JNX; EM; 4.08 A; D=1-1407.
DR PDB; 6K4Y; EM; 3.79 A; D=1-1407.
DR PDB; 6KJ6; EM; 3.80 A; D=1-1407.
DR PDB; 6LDI; EM; 3.69 A; D=1-1407.
DR PDB; 6N4C; EM; 17.00 A; D=15-1376.
DR PDB; 6N57; EM; 3.70 A; J=2-1407.
DR PDB; 6N58; EM; 3.78 A; J=2-1407.
DR PDB; 6N60; X-ray; 3.68 A; D=2-1407.
DR PDB; 6N61; X-ray; 3.25 A; D=2-1407.
DR PDB; 6OMF; EM; 3.26 A; D=1-1407.
DR PDB; 6P18; EM; 3.50 A; D=1-1407.
DR PDB; 6P19; EM; 3.80 A; D=1-1407.
DR PDB; 6P1K; EM; 4.05 A; J=2-1407.
DR PDB; 6PSQ; EM; 3.40 A; J=2-1407.
DR PDB; 6PSR; EM; 3.40 A; J=2-1407.
DR PDB; 6PSS; EM; 3.50 A; J=2-1407.
DR PDB; 6PST; EM; 3.00 A; J=2-1407.
DR PDB; 6PSU; EM; 3.90 A; J=2-1407.
DR PDB; 6PSV; EM; 3.50 A; J=2-1407.
DR PDB; 6PSW; EM; 3.70 A; J=2-1407.
DR PDB; 6R9B; EM; 3.80 A; D=1-1407.
DR PDB; 6R9G; EM; 3.70 A; D=1-1407.
DR PDB; 6RH3; EM; 3.60 A; D=1-1407.
DR PDB; 6RI7; EM; 3.90 A; D=1-1407.
DR PDB; 6RI9; EM; 3.70 A; D=1-1407.
DR PDB; 6RIN; EM; 3.70 A; D=1-1407.
DR PDB; 6RIP; EM; 3.40 A; D=1-1407.
DR PDB; 6TQN; EM; 3.80 A; Y=1-1407.
DR PDB; 6TQO; EM; 4.00 A; Y=1-1407.
DR PDB; 6UTV; X-ray; 3.45 A; DDD=1-1407.
DR PDB; 6UTW; X-ray; 3.85 A; DDD=1-1407.
DR PDB; 6UTX; X-ray; 4.05 A; DDD=1-1407.
DR PDB; 6UTY; X-ray; 4.15 A; DDD=1-1407.
DR PDB; 6UTZ; X-ray; 3.80 A; DDD=1-1407.
DR PDB; 6UU0; X-ray; 3.90 A; DDD=1-1407.
DR PDB; 6UU1; X-ray; 4.10 A; DDD=1-1407.
DR PDB; 6UU2; X-ray; 4.40 A; DDD=1-1407.
DR PDB; 6UU3; X-ray; 4.00 A; DDD=1-1407.
DR PDB; 6UU4; X-ray; 4.30 A; DDD=1-1407.
DR PDB; 6UU5; X-ray; 5.40 A; DDD=1-1407.
DR PDB; 6UU6; X-ray; 4.20 A; DDD=1-1407.
DR PDB; 6UU7; X-ray; 4.40 A; DDD=1-1407.
DR PDB; 6UU8; X-ray; 4.40 A; DDD=1-1407.
DR PDB; 6UU9; X-ray; 5.40 A; DDD=1-1407.
DR PDB; 6UUA; X-ray; 4.00 A; DDD=1-1407.
DR PDB; 6UUB; X-ray; 3.96 A; DDD=1-1407.
DR PDB; 6UUC; X-ray; 4.10 A; DDD=1-1407.
DR PDB; 6VJS; X-ray; 4.02 A; D/I=1-1407.
DR PDB; 6WMU; EM; 3.18 A; D=1-1407.
DR PDB; 6X26; EM; 4.10 A; J=1-1407.
DR PDB; 6X2F; EM; 4.00 A; J=1-1407.
DR PDB; 6X2N; EM; 3.90 A; J=1-1407.
DR PDB; 6X43; EM; 3.60 A; J=1-1407.
DR PDB; 6X4W; EM; 3.80 A; J=1-1407.
DR PDB; 6X4Y; EM; 3.60 A; J=1-1407.
DR PDB; 6X50; EM; 3.30 A; J=1-1407.
DR PDB; 6XAS; EM; 3.80 A; J=2-1407.
DR PDB; 6XAV; EM; 7.70 A; J=2-1407.
DR PDB; 6XH7; EM; 3.90 A; D=1-1407.
DR PDB; 6XH8; EM; 4.10 A; D=1-1407.
DR PDB; 6XL5; EM; 2.50 A; D=1-1407.
DR PDB; 6XL9; EM; 2.50 A; D=1-1407.
DR PDB; 6XLJ; EM; 2.70 A; D=1-1407.
DR PDB; 6XLL; EM; 2.70 A; D=1-1407.
DR PDB; 6XLM; EM; 3.20 A; D=1-1407.
DR PDB; 6XLN; EM; 2.80 A; D=1-1407.
DR PDB; 6Z9P; EM; 3.90 A; Y=1-1407.
DR PDB; 6Z9Q; EM; 5.70 A; Y=1-1407.
DR PDB; 6Z9R; EM; 4.10 A; Y=1-1407.
DR PDB; 6Z9S; EM; 4.40 A; Y=1-1407.
DR PDB; 6Z9T; EM; 4.10 A; Y=1-1407.
DR PDB; 7ADB; EM; 4.40 A; Y=1-1407.
DR PDB; 7ADC; EM; 4.00 A; Y=1-1407.
DR PDB; 7ADD; EM; 4.30 A; Y=1-1407.
DR PDB; 7ADE; EM; 4.20 A; Y=1-1407.
DR PDB; 7BEF; EM; 4.50 A; D=1-1407.
DR PDB; 7C17; EM; 4.22 A; D=1-1407.
DR PDB; 7C97; EM; 3.68 A; D=1-1407.
DR PDB; 7CHW; EM; 3.58 A; D=1-1407.
DR PDB; 7DY6; EM; 3.68 A; D=1-1407.
DR PDB; 7KHB; EM; 3.53 A; D=1-1407.
DR PDB; 7KHC; EM; 4.14 A; D=1-1407.
DR PDB; 7KHE; EM; 3.58 A; D=1-1407.
DR PDB; 7KHI; EM; 3.62 A; D=1-1407.
DR PDB; 7M8E; EM; 3.40 A; D=1-1407.
DR PDB; 7MKN; EM; 3.30 A; D=14-1376.
DR PDB; 7MKO; EM; 3.15 A; D=14-1376.
DR PDB; 7MKP; EM; 3.41 A; D=14-1376.
DR PDB; 7MKQ; EM; 4.80 A; D=14-1376.
DR PDBsum; 2AUK; -.
DR PDBsum; 2LMC; -.
DR PDBsum; 3IYD; -.
DR PDBsum; 3LU0; -.
DR PDBsum; 4IQZ; -.
DR PDBsum; 4JK1; -.
DR PDBsum; 4JK2; -.
DR PDBsum; 4KMU; -.
DR PDBsum; 4KN4; -.
DR PDBsum; 4KN7; -.
DR PDBsum; 4MEX; -.
DR PDBsum; 4MEY; -.
DR PDBsum; 4XSX; -.
DR PDBsum; 4XSY; -.
DR PDBsum; 4XSZ; -.
DR PDBsum; 4YG2; -.
DR PDBsum; 4YLN; -.
DR PDBsum; 4YLO; -.
DR PDBsum; 4YLP; -.
DR PDBsum; 4ZH2; -.
DR PDBsum; 4ZH3; -.
DR PDBsum; 4ZH4; -.
DR PDBsum; 5BYH; -.
DR PDBsum; 5EZK; -.
DR PDBsum; 5IPL; -.
DR PDBsum; 5IPM; -.
DR PDBsum; 5IPN; -.
DR PDBsum; 5MS0; -.
DR PDBsum; 5MY1; -.
DR PDBsum; 5NSR; -.
DR PDBsum; 5NSS; -.
DR PDBsum; 5NWT; -.
DR PDBsum; 5UAC; -.
DR PDBsum; 5UAG; -.
DR PDBsum; 5UAH; -.
DR PDBsum; 5UAJ; -.
DR PDBsum; 5UAL; -.
DR PDBsum; 5UAQ; -.
DR PDBsum; 5VSW; -.
DR PDBsum; 5VT0; -.
DR PDBsum; 5W1S; -.
DR PDBsum; 5W1T; -.
DR PDBsum; 6ALF; -.
DR PDBsum; 6ALG; -.
DR PDBsum; 6ALH; -.
DR PDBsum; 6ASX; -.
DR PDBsum; 6BJS; -.
DR PDBsum; 6BYU; -.
DR PDBsum; 6C6S; -.
DR PDBsum; 6C6T; -.
DR PDBsum; 6C6U; -.
DR PDBsum; 6C9Y; -.
DR PDBsum; 6CA0; -.
DR PDBsum; 6CUX; -.
DR PDBsum; 6FLP; -.
DR PDBsum; 6FLQ; -.
DR PDBsum; 6GFW; -.
DR PDBsum; 6GH5; -.
DR PDBsum; 6GH6; -.
DR PDBsum; 6JBQ; -.
DR PDBsum; 6JNX; -.
DR PDBsum; 6K4Y; -.
DR PDBsum; 6KJ6; -.
DR PDBsum; 6LDI; -.
DR PDBsum; 6N4C; -.
DR PDBsum; 6N57; -.
DR PDBsum; 6N58; -.
DR PDBsum; 6N60; -.
DR PDBsum; 6N61; -.
DR PDBsum; 6OMF; -.
DR PDBsum; 6P18; -.
DR PDBsum; 6P19; -.
DR PDBsum; 6P1K; -.
DR PDBsum; 6PSQ; -.
DR PDBsum; 6PSR; -.
DR PDBsum; 6PSS; -.
DR PDBsum; 6PST; -.
DR PDBsum; 6PSU; -.
DR PDBsum; 6PSV; -.
DR PDBsum; 6PSW; -.
DR PDBsum; 6R9B; -.
DR PDBsum; 6R9G; -.
DR PDBsum; 6RH3; -.
DR PDBsum; 6RI7; -.
DR PDBsum; 6RI9; -.
DR PDBsum; 6RIN; -.
DR PDBsum; 6RIP; -.
DR PDBsum; 6TQN; -.
DR PDBsum; 6TQO; -.
DR PDBsum; 6UTV; -.
DR PDBsum; 6UTW; -.
DR PDBsum; 6UTX; -.
DR PDBsum; 6UTY; -.
DR PDBsum; 6UTZ; -.
DR PDBsum; 6UU0; -.
DR PDBsum; 6UU1; -.
DR PDBsum; 6UU2; -.
DR PDBsum; 6UU3; -.
DR PDBsum; 6UU4; -.
DR PDBsum; 6UU5; -.
DR PDBsum; 6UU6; -.
DR PDBsum; 6UU7; -.
DR PDBsum; 6UU8; -.
DR PDBsum; 6UU9; -.
DR PDBsum; 6UUA; -.
DR PDBsum; 6UUB; -.
DR PDBsum; 6UUC; -.
DR PDBsum; 6VJS; -.
DR PDBsum; 6WMU; -.
DR PDBsum; 6X26; -.
DR PDBsum; 6X2F; -.
DR PDBsum; 6X2N; -.
DR PDBsum; 6X43; -.
DR PDBsum; 6X4W; -.
DR PDBsum; 6X4Y; -.
DR PDBsum; 6X50; -.
DR PDBsum; 6XAS; -.
DR PDBsum; 6XAV; -.
DR PDBsum; 6XH7; -.
DR PDBsum; 6XH8; -.
DR PDBsum; 6XL5; -.
DR PDBsum; 6XL9; -.
DR PDBsum; 6XLJ; -.
DR PDBsum; 6XLL; -.
DR PDBsum; 6XLM; -.
DR PDBsum; 6XLN; -.
DR PDBsum; 6Z9P; -.
DR PDBsum; 6Z9Q; -.
DR PDBsum; 6Z9R; -.
DR PDBsum; 6Z9S; -.
DR PDBsum; 6Z9T; -.
DR PDBsum; 7ADB; -.
DR PDBsum; 7ADC; -.
DR PDBsum; 7ADD; -.
DR PDBsum; 7ADE; -.
DR PDBsum; 7BEF; -.
DR PDBsum; 7C17; -.
DR PDBsum; 7C97; -.
DR PDBsum; 7CHW; -.
DR PDBsum; 7DY6; -.
DR PDBsum; 7KHB; -.
DR PDBsum; 7KHC; -.
DR PDBsum; 7KHE; -.
DR PDBsum; 7KHI; -.
DR PDBsum; 7M8E; -.
DR PDBsum; 7MKN; -.
DR PDBsum; 7MKO; -.
DR PDBsum; 7MKP; -.
DR PDBsum; 7MKQ; -.
DR AlphaFoldDB; P0A8T7; -.
DR SMR; P0A8T7; -.
DR BioGRID; 4262959; 70.
DR ComplexPortal; CPX-4881; DNA-directed RNA polymerase holoenzyme complex, Sigma70 variant.
DR ComplexPortal; CPX-4883; DNA-directed RNA polymerase holoenzyme complex, SigmaS variant.
DR ComplexPortal; CPX-4884; DNA-directed RNA polymerase holoenzyme complex, Sigma54 variant.
DR ComplexPortal; CPX-4885; DNA-directed RNA polymerase holoenzyme complex, SigmaE variant.
DR ComplexPortal; CPX-4886; DNA-directed RNA polymerase holoenzyme complex, SigmaF variant.
DR ComplexPortal; CPX-4887; DNA-directed RNA polymerase holoenzyme complex, SigmaH variant.
DR ComplexPortal; CPX-4888; DNA-directed RNA polymerase holoenzyme complex, Sigma fecI variant.
DR ComplexPortal; CPX-5674; Transcription elongation complex.
DR ComplexPortal; CPX-5780; lambdaN-dependent processive transcription antitermination complex.
DR DIP; DIP-35803N; -.
DR IntAct; P0A8T7; 117.
DR MINT; P0A8T7; -.
DR STRING; 511145.b3988; -.
DR BindingDB; P0A8T7; -.
DR ChEMBL; CHEMBL2364672; -.
DR ChEMBL; CHEMBL4296169; -.
DR DrugBank; DB00615; Rifabutin.
DR DrugBank; DB11753; Rifamycin.
DR DrugCentral; P0A8T7; -.
DR iPTMnet; P0A8T7; -.
DR jPOST; P0A8T7; -.
DR PaxDb; P0A8T7; -.
DR PRIDE; P0A8T7; -.
DR ABCD; P0A8T7; 1 sequenced antibody.
DR EnsemblBacteria; AAC76962; AAC76962; b3988.
DR EnsemblBacteria; BAE77332; BAE77332; BAE77332.
DR GeneID; 66672101; -.
DR GeneID; 948487; -.
DR KEGG; ecj:JW3951; -.
DR KEGG; eco:b3988; -.
DR PATRIC; fig|1411691.4.peg.2724; -.
DR EchoBASE; EB0888; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_6; -.
DR InParanoid; P0A8T7; -.
DR OMA; YRNIRVE; -.
DR PhylomeDB; P0A8T7; -.
DR BioCyc; EcoCyc:RPOC-MON; -.
DR BioCyc; MetaCyc:RPOC-MON; -.
DR BRENDA; 2.7.7.6; 2026.
DR EvolutionaryTrace; P0A8T7; -.
DR PRO; PR:P0A8T7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0000345; C:cytosolic DNA-directed RNA polymerase complex; IPI:ComplexPortal.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0008023; C:transcription elongation factor complex; IC:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044780; P:bacterial-type flagellum assembly; IC:ComplexPortal.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IC:ComplexPortal.
DR GO; GO:0048870; P:cell motility; IC:ComplexPortal.
DR GO; GO:0036460; P:cellular response to cell envelope stress; IC:ComplexPortal.
DR GO; GO:0055072; P:iron ion homeostasis; IC:ComplexPortal.
DR GO; GO:0042128; P:nitrate assimilation; IC:ComplexPortal.
DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IC:ComplexPortal.
DR GO; GO:2000142; P:regulation of DNA-templated transcription, initiation; IDA:ComplexPortal.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0009408; P:response to heat; IC:ComplexPortal.
DR GO; GO:0090605; P:submerged biofilm formation; IC:ComplexPortal.
DR GO; GO:0031564; P:transcription antitermination; IDA:ComplexPortal.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR012754; DNA-dir_RpoC_beta_prime_bact.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
DR TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Antibiotic resistance;
KW Direct protein sequencing; DNA-directed RNA polymerase; Magnesium;
KW Metal-binding; Nucleotidyltransferase; Reference proteome; Transcription;
KW Transferase; Zinc.
FT CHAIN 1..1407
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067741"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:32871103,
FT ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:32871103,
FT ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:32871103,
FT ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:32871103,
FT ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:32871103,
FT ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:32871103,
FT ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:32871103,
FT ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY"
FT BINDING 814
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:32871103,
FT ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY"
FT BINDING 888
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:32871103,
FT ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY"
FT BINDING 895
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:32871103,
FT ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY"
FT BINDING 898
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:32871103,
FT ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY"
FT MOD_RES 983
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322,
FT ECO:0000269|PubMed:18723842"
FT MUTAGEN 504
FT /note="Q->P: Resistant to antibiotics salinamide A and B."
FT /evidence="ECO:0000269|PubMed:24843001"
FT MUTAGEN 690
FT /note="N->D: Resistant to antibiotics salinamide A and B."
FT /evidence="ECO:0000269|PubMed:24843001"
FT MUTAGEN 697
FT /note="M->V: Resistant to antibiotics salinamide A and B."
FT /evidence="ECO:0000269|PubMed:24843001"
FT MUTAGEN 735
FT /note="A->T: Resistant to antibiotics salinamide A and B."
FT /evidence="ECO:0000269|PubMed:24843001"
FT MUTAGEN 738
FT /note="R->C,H,P,S: Resistant to antibiotics salinamide A
FT and B."
FT /evidence="ECO:0000269|PubMed:24843001"
FT MUTAGEN 748
FT /note="A->E: Resistant to antibiotics salinamide A and B."
FT /evidence="ECO:0000269|PubMed:24843001"
FT MUTAGEN 758
FT /note="P->S,T: Resistant to antibiotics salinamide A and
FT B."
FT /evidence="ECO:0000269|PubMed:24843001"
FT MUTAGEN 763
FT /note="F->C: Resistant to antibiotics salinamide A and B."
FT /evidence="ECO:0000269|PubMed:24843001"
FT MUTAGEN 775
FT /note="S->A: Resistant to antibiotics salinamide A and B."
FT /evidence="ECO:0000269|PubMed:24843001"
FT MUTAGEN 779
FT /note="A->T,V: Resistant to antibiotics salinamide A and
FT B."
FT /evidence="ECO:0000269|PubMed:24843001"
FT MUTAGEN 780
FT /note="R->C: Resistant to antibiotics salinamide A and B."
FT /evidence="ECO:0000269|PubMed:24843001"
FT MUTAGEN 782
FT /note="G->A,C: Resistant to antibiotics salinamide A and
FT B."
FT /evidence="ECO:0000269|PubMed:24843001"
FT MUTAGEN 783
FT /note="L->R: Resistant to antibiotics salinamide A and B."
FT /evidence="ECO:0000269|PubMed:24843001"
FT CONFLICT 1133..1177
FT /note="DITGGLPRVADLFEARRPKEPAILAEISGIVSFGKETKGKRRLVI -> ASP
FT VVCRALRTCSKHVVRKSRQSWLKSAVSFPSVKKPKVNVVWLS (in Ref. 11; no
FT nucleotide entry)"
FT /evidence="ECO:0000305"
FT HELIX 5..12
FT /evidence="ECO:0007829|PDB:6WMU"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:6GH5"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:6XL9"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:6XLJ"
FT HELIX 95..99
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 102..112
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 132..139
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:6PSS"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 194..205
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 211..229
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 238..244
FT /evidence="ECO:0007829|PDB:6XL5"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:6XL9"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:6XLN"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 264..285
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 289..307
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 327..331
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:6WMU"
FT HELIX 337..341
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 343..357
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:6GH5"
FT STRAND 365..369
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 370..376
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 378..387
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:6PST"
FT HELIX 394..403
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 406..415
FT /evidence="ECO:0007829|PDB:6XL5"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:6XLJ"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 434..449
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 454..457
FT /evidence="ECO:0007829|PDB:6XL5"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 465..469
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 474..482
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:6RIP"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 493..500
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 505..513
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:6XL5"
FT TURN 521..524
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 526..529
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 530..538
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 546..557
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 559..561
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 563..573
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 574..580
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:6GH5"
FT HELIX 589..591
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 592..594
FT /evidence="ECO:0007829|PDB:6N61"
FT HELIX 598..612
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 614..635
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 641..643
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 650..669
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 675..702
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 703..709
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 712..716
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 721..727
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 728..731
FT /evidence="ECO:0007829|PDB:6PST"
FT HELIX 734..741
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 745..748
FT /evidence="ECO:0007829|PDB:6PST"
FT STRAND 750..752
FT /evidence="ECO:0007829|PDB:6XLN"
FT STRAND 754..759
FT /evidence="ECO:0007829|PDB:6PST"
FT STRAND 763..765
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 769..804
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 809..812
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 820..822
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 825..828
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 830..833
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 835..839
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 840..842
FT /evidence="ECO:0007829|PDB:6GH5"
FT STRAND 843..846
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 851..853
FT /evidence="ECO:0007829|PDB:6XL9"
FT STRAND 856..858
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 866..874
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 880..882
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 885..887
FT /evidence="ECO:0007829|PDB:6XLL"
FT STRAND 893..895
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 896..899
FT /evidence="ECO:0007829|PDB:6XL5"
FT TURN 903..905
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 906..908
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 915..924
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 925..929
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 945..948
FT /evidence="ECO:0007829|PDB:2AUK"
FT STRAND 949..951
FT /evidence="ECO:0007829|PDB:4IQZ"
FT STRAND 956..962
FT /evidence="ECO:0007829|PDB:4IQZ"
FT STRAND 965..967
FT /evidence="ECO:0007829|PDB:4IQZ"
FT STRAND 969..971
FT /evidence="ECO:0007829|PDB:6XLL"
FT STRAND 973..975
FT /evidence="ECO:0007829|PDB:4IQZ"
FT STRAND 977..979
FT /evidence="ECO:0007829|PDB:6PSR"
FT STRAND 981..985
FT /evidence="ECO:0007829|PDB:4IQZ"
FT STRAND 987..989
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 991..996
FT /evidence="ECO:0007829|PDB:4IQZ"
FT STRAND 1002..1005
FT /evidence="ECO:0007829|PDB:4IQZ"
FT STRAND 1007..1010
FT /evidence="ECO:0007829|PDB:6N61"
FT STRAND 1013..1015
FT /evidence="ECO:0007829|PDB:6GH5"
FT STRAND 1016..1019
FT /evidence="ECO:0007829|PDB:4IQZ"
FT STRAND 1022..1028
FT /evidence="ECO:0007829|PDB:4IQZ"
FT STRAND 1030..1032
FT /evidence="ECO:0007829|PDB:6XL9"
FT STRAND 1033..1039
FT /evidence="ECO:0007829|PDB:4IQZ"
FT TURN 1043..1045
FT /evidence="ECO:0007829|PDB:4IQZ"
FT STRAND 1046..1049
FT /evidence="ECO:0007829|PDB:4IQZ"
FT TURN 1052..1054
FT /evidence="ECO:0007829|PDB:2AUK"
FT STRAND 1058..1061
FT /evidence="ECO:0007829|PDB:4IQZ"
FT HELIX 1064..1066
FT /evidence="ECO:0007829|PDB:4IQZ"
FT HELIX 1071..1073
FT /evidence="ECO:0007829|PDB:4IQZ"
FT STRAND 1077..1081
FT /evidence="ECO:0007829|PDB:4IQZ"
FT STRAND 1085..1087
FT /evidence="ECO:0007829|PDB:6XL9"
FT STRAND 1093..1096
FT /evidence="ECO:0007829|PDB:4IQZ"
FT STRAND 1098..1100
FT /evidence="ECO:0007829|PDB:4IQZ"
FT STRAND 1106..1109
FT /evidence="ECO:0007829|PDB:2AUK"
FT STRAND 1113..1115
FT /evidence="ECO:0007829|PDB:6OMF"
FT STRAND 1120..1125
FT /evidence="ECO:0007829|PDB:4IQZ"
FT STRAND 1135..1137
FT /evidence="ECO:0007829|PDB:6PSS"
FT HELIX 1138..1145
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 1161..1165
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 1169..1178
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 1180..1182
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 1187..1191
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 1192..1194
FT /evidence="ECO:0007829|PDB:6PST"
FT STRAND 1200..1204
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 1209..1211
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 1217..1223
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 1226..1243
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 1251..1260
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 1263..1268
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 1270..1273
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 1276..1278
FT /evidence="ECO:0007829|PDB:6GH5"
FT STRAND 1279..1281
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 1282..1292
FT /evidence="ECO:0007829|PDB:6XL5"
FT TURN 1293..1296
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 1301..1304
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 1309..1313
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 1315..1317
FT /evidence="ECO:0007829|PDB:6P18"
FT HELIX 1319..1325
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 1328..1338
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 1341..1343
FT /evidence="ECO:0007829|PDB:6RIP"
FT HELIX 1347..1352
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 1360..1362
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 1363..1371
FT /evidence="ECO:0007829|PDB:6XL5"
SQ SEQUENCE 1407 AA; 155160 MW; A6878C61D15F4961 CRC64;
MKDLLKFLKA QTKTEEFDAI KIALASPDMI RSWSFGEVKK PETINYRTFK PERDGLFCAR
IFGPVKDYEC LCGKYKRLKH RGVICEKCGV EVTQTKVRRE RMGHIELASP TAHIWFLKSL
PSRIGLLLDM PLRDIERVLY FESYVVIEGG MTNLERQQIL TEEQYLDALE EFGDEFDAKM
GAEAIQALLK SMDLEQECEQ LREELNETNS ETKRKKLTKR IKLLEAFVQS GNKPEWMILT
VLPVLPPDLR PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLLDLAAPDI IVRNEKRMLQ
EAVDALLDNG RRGRAITGSN KRPLKSLADM IKGKQGRFRQ NLLGKRVDYS GRSVITVGPY
LRLHQCGLPK KMALELFKPF IYGKLELRGL ATTIKAAKKM VEREEAVVWD ILDEVIREHP
VLLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCAAYNAD FDGDQMAVHV PLTLEAQLEA
RALMMSTNNI LSPANGEPII VPSQDVVLGL YYMTRDCVNA KGEGMVLTGP KEAERLYRSG
LASLHARVKV RITEYEKDAN GELVAKTSLK DTTVGRAILW MIVPKGLPYS IVNQALGKKA
ISKMLNTCYR ILGLKPTVIF ADQIMYTGFA YAARSGASVG IDDMVIPEKK HEIISEAEAE
VAEIQEQFQS GLVTAGERYN KVIDIWAAAN DRVSKAMMDN LQTETVINRD GQEEKQVSFN
SIYMMADSGA RGSAAQIRQL AGMRGLMAKP DGSIIETPIT ANFREGLNVL QYFISTHGAR
KGLADTALKT ANSGYLTRRL VDVAQDLVVT EDDCGTHEGI MMTPVIEGGD VKEPLRDRVL
GRVTAEDVLK PGTADILVPR NTLLHEQWCD LLEENSVDAV KVRSVVSCDT DFGVCAHCYG
RDLARGHIIN KGEAIGVIAA QSIGEPGTQL TMRTFHIGGA ASRAAAESSI QVKNKGSIKL
SNVKSVVNSS GKLVITSRNT ELKLIDEFGR TKESYKVPYG AVLAKGDGEQ VAGGETVANW
DPHTMPVITE VSGFVRFTDM IDGQTITRQT DELTGLSSLV VLDSAERTAG GKDLRPALKI
VDAQGNDVLI PGTDMPAQYF LPGKAIVQLE DGVQISSGDT LARIPQESGG TKDITGGLPR
VADLFEARRP KEPAILAEIS GIVSFGKETK GKRRLVITPV DGSDPYEEMI PKWRQLNVFE
GERVERGDVI SDGPEAPHDI LRLRGVHAVT RYIVNEVQDV YRLQGVKIND KHIEVIVRQM
LRKATIVNAG SSDFLEGEQV EYSRVKIANR ELEANGKVGA TYSRDLLGIT KASLATESFI
SAASFQETTR VLTEAAVAGK RDELRGLKEN VIVGRLIPAG TGYAYHQDRM RRRAAGEAPA
APQVTAEDAS ASLAELLNAG LGGSDNE
