RPOB_ECOLI
ID RPOB_ECOLI Reviewed; 1342 AA.
AC P0A8V2; P00575; P00576; P78242; Q2M8S3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=DNA-directed RNA polymerase subunit beta;
DE Short=RNAP subunit beta;
DE EC=2.7.7.6;
DE AltName: Full=RNA polymerase subunit beta;
DE AltName: Full=Transcriptase subunit beta;
GN Name=rpoB; Synonyms=groN, nitB, rif, ron, stl, stv, tabD;
GN OrderedLocusNames=b3987, JW3950;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B;
RA Miller E.S., Shih G.C., Chung S.K., Ballard D.N.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-391.
RX PubMed=7011900; DOI=10.1016/0378-1119(80)90076-1;
RA Delcuve G., Downing W., Lewis H., Dennis P.P.;
RT "Nucleotide sequence of the proximal portion of the RNA polymerase beta
RT subunit gene of Escherichia coli.";
RL Gene 11:367-373(1980).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-188.
RA Gurevich A.I., Avakov A.E., Kolosov M.N.;
RT "The nucleotide sequence at the proximal end of rpoB gene of Escherichia
RT coli.";
RL Bioorg. Khim. 5:1735-1739(1979).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-188.
RA Monastyrskaya G.S., Gubanov V.V., Guryev S.O., Lipkin V.M., Sverdlov E.D.;
RT "Primary structure of RNA polymerase from E.coli: nucleotide sequence of
RT the rpoB gene fragment and corresponding N-terminal amino acid sequence of
RT the beta-subunit.";
RL Bioorg. Khim. 6:1423-1426(1980).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
RX PubMed=377281; DOI=10.1073/pnas.76.4.1697;
RA Post L.E., Strycharz G.D., Nomura M., Lewis H., Dennis P.P.;
RT "Nucleotide sequence of the ribosomal protein gene cluster adjacent to the
RT gene for RNA polymerase subunit beta in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:1697-1701(1979).
RN [10]
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 [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 187-1144.
RA Ovchinnikov Y.A., Sverdlov E.D., Lipkin V.M., Monastyrskaya G.S.,
RA Chertov O.Y., Gubanov V.V., Guryev S.O., Modyanov N.N., Grinkevich V.A.,
RA Makarova I.A., Marchenko T.V., Polovnikova I.N.;
RT "Primary structure of RNA polymerase from E. coli; nucleotide sequence of
RT EcoR1-C fragment of gene rpoB and amino acid sequence of the corresponding
RT fragment of beta-subunit.";
RL Bioorg. Khim. 6:655-665(1980).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 187-354.
RA Sverdlov E.D., Lipkin V.M., Monastyrskaya G.S., Gubanov V.V., Guryev S.O.,
RA Chertov O.Y.;
RT "The nucleotide sequence of strong RNA polymerase binding site within the
RT E.coli rpoB structural gene.";
RL Bioorg. Khim. 6:309-312(1980).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 500-669.
RC STRAIN=ATCC 25290;
RA Mollet C., Drancourt M., Raoult D.;
RT "RNA polymerase beta-subunit.";
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1143-1342.
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 [15]
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 [16]
RP MUTAGENESIS OF GLU-813.
RX PubMed=2068078; DOI=10.1073/pnas.88.14.6018;
RA Lee J., Kashlev M., Borukhov S., Goldfarb A.;
RT "A beta subunit mutation disrupting the catalytic function of Escherichia
RT coli RNA polymerase.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6018-6022(1991).
RN [17]
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 [18]
RP INTERACTION WITH ESCHERICHIA PHAGE LAMBDA ANTITERMINATION PROTEIN Q
RP (MICROBIAL INFECTION).
RX PubMed=18832144; DOI=10.1073/pnas.0805757105;
RA Deighan P., Diez C.M., Leibman M., Hochschild A., Nickels B.E.;
RT "The bacteriophage lambda Q antiterminator protein contacts the beta-flap
RT domain of RNA polymerase.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15305-15310(2008).
RN [19]
RP INTERACTION WITH ESCHERICHIA PHAGE LAMBDA ANTITERMINATION PROTEIN Q
RP (MICROBIAL INFECTION).
RX PubMed=32313022; DOI=10.1038/s41598-020-63523-5;
RA Dudenhoeffer B.R., Borggraefe J., Schweimer K., Knauer S.H.;
RT "NusA directly interacts with antitermination factor Q from phage lambda.";
RL Sci. Rep. 10:6607-6607(2020).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1022 AND LYS-1200, AND
RP IDENTIFICATION BY MASS 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 [21]
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 [22] {ECO:0007744|PDB:3IYD}
RP STRUCTURE BY ELECTRON MICROSCOPY (19.80 ANGSTROMS) IN COMPLEX WITH RPOA;
RP RPOC; 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 [23] {ECO:0007744|PDB:3TBI}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 831-1057, AND INTERACTION WITH
RP ENTEROBACTERIA PHAGE T4 RNA POLYMERASE COACTIVATOR (MICROBIAL INFECTION).
RX PubMed=22135460; DOI=10.1073/pnas.1113328108;
RA Twist K.A., Campbell E.A., Deighan P., Nechaev S., Jain V.,
RA Geiduschek E.P., Hochschild A., Darst S.A.;
RT "Crystal structure of the bacteriophage T4 late-transcription coactivator
RT gp33 with the beta-subunit flap domain of Escherichia coli RNA
RT polymerase.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:19961-19966(2011).
RN [24] {ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY}
RP X-RAY CRYSTALLOGRAPHY (3.90 ANGSTROMS) IN COMPLEX WITH RPOA; RPOC; RPOD;
RP RPOZ AND SALINAMIDE A, FUNCTION, SUBUNIT, BIOTECHNOLOGY, ANTIBIOTIC
RP RESISTANCE, AND MUTAGENESIS OF ILE-561; ILE-569; ALA-665; ASP-675; ASN-677
RP AND LEU-680.
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 [25] {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,
RP FUNCTION, AND SUBUNIT.
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:0000269|PubMed:1646077,
CC 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;
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:0000269|PubMed:1646077,
CC ECO:0000269|PubMed:19903881, ECO:0000269|PubMed:24843001,
CC ECO:0000269|PubMed:32871103}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via flap domain) with
CC Escherichia phage lambda antitermination protein Q; this interaction
CC renders bacterial RNAP resistant to transcription pausing and allows it
CC to read through termination signals. {ECO:0000269|PubMed:18832144,
CC ECO:0000269|PubMed:32313022}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via flap domain) with the
CC late transcription coactivator of enterobacteria phage T4.
CC {ECO:0000269|PubMed:22135460}.
CC -!- INTERACTION:
CC P0A8V2; P60240: rapA; NbExp=5; IntAct=EBI-544996, EBI-551542;
CC P0A8V2; P0A8T7: rpoC; NbExp=11; IntAct=EBI-544996, EBI-543604;
CC P0A8V2; P00579: rpoD; NbExp=10; IntAct=EBI-544996, EBI-545104;
CC P0A8V2; P13445: rpoS; NbExp=5; IntAct=EBI-544996, EBI-557581;
CC P0A8V2; P03018: uvrD; NbExp=3; IntAct=EBI-544996, EBI-559573;
CC P0A8V2; P13338: 33; Xeno; NbExp=5; IntAct=EBI-544996, EBI-15955782;
CC P0A8V2; P32267: asiA; Xeno; NbExp=4; IntAct=EBI-544996, EBI-2124737;
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:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=Ref.7; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR EMBL; V00339; CAA23625.1; -; Genomic_DNA.
DR EMBL; V00340; CAA23627.1; -; Genomic_DNA.
DR EMBL; U76222; AAB18647.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43085.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76961.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77333.1; -; Genomic_DNA.
DR EMBL; V00341; CAA23629.1; -; Genomic_DNA.
DR EMBL; M38292; AAA24579.1; -; Genomic_DNA.
DR EMBL; M38293; AAA24581.1; -; Genomic_DNA.
DR EMBL; M38287; AAA24585.1; -; Genomic_DNA.
DR EMBL; M38304; AAA24580.1; -; Genomic_DNA.
DR EMBL; U77436; AAD09605.1; -; Genomic_DNA.
DR EMBL; M38303; AAA24583.1; -; Genomic_DNA.
DR PIR; F65205; RNECB.
DR RefSeq; NP_418414.1; NC_000913.3.
DR RefSeq; WP_000263098.1; NZ_STEB01000045.1.
DR PDB; 3IYD; EM; -; C=1-1342.
DR PDB; 3LTI; X-ray; 1.60 A; A=152-443.
DR PDB; 3LU0; EM; -; C=1-1342.
DR PDB; 3T72; X-ray; 4.33 A; o/q=896-910.
DR PDB; 3TBI; X-ray; 3.00 A; B=831-1057.
DR PDB; 4JK1; X-ray; 3.90 A; C/H=1-1342.
DR PDB; 4JK2; X-ray; 4.20 A; C/H=1-1342.
DR PDB; 4KMU; X-ray; 3.85 A; C/H=1-1342.
DR PDB; 4KN4; X-ray; 3.96 A; C/H=1-1342.
DR PDB; 4KN7; X-ray; 3.69 A; C/H=1-1342.
DR PDB; 4MEX; X-ray; 3.90 A; C/I=1-1342.
DR PDB; 4MEY; X-ray; 3.95 A; C/I=1-1342.
DR PDB; 4S20; X-ray; 4.70 A; C/H=1-1342.
DR PDB; 4XSX; X-ray; 3.71 A; C/I=1-1342.
DR PDB; 4XSY; X-ray; 4.01 A; C/I=1-1342.
DR PDB; 4XSZ; X-ray; 3.68 A; C/I=1-1342.
DR PDB; 4YG2; X-ray; 3.70 A; C/I=1-1342.
DR PDB; 4YLN; X-ray; 5.50 A; C/I/O=1-1342.
DR PDB; 4YLO; X-ray; 6.00 A; C/I/O=1-1342.
DR PDB; 4YLP; X-ray; 5.50 A; C/I/O=1-1342.
DR PDB; 4ZH2; X-ray; 4.20 A; C/I=1-1342.
DR PDB; 4ZH3; X-ray; 4.08 A; C/I=1-1342.
DR PDB; 4ZH4; X-ray; 3.99 A; C/I=1-1342.
DR PDB; 5BYH; X-ray; 3.76 A; C=1-1342.
DR PDB; 5EZK; X-ray; 8.50 A; C=1-1342.
DR PDB; 5IPL; X-ray; 3.60 A; C=1-1342.
DR PDB; 5IPM; X-ray; 4.20 A; C=1-1342.
DR PDB; 5IPN; X-ray; 4.61 A; C=1-1342.
DR PDB; 5MS0; EM; 9.80 A; C=1-1342.
DR PDB; 5MY1; EM; 7.60 A; X=1-1342.
DR PDB; 5NSR; EM; 3.80 A; C=1-1342.
DR PDB; 5NSS; EM; 5.80 A; C=1-1342.
DR PDB; 5NWT; X-ray; 3.76 A; C=1-1342.
DR PDB; 5UAC; X-ray; 3.80 A; C/I=1-1342.
DR PDB; 5UAG; X-ray; 3.40 A; C/I=1-1342.
DR PDB; 5UAH; X-ray; 4.10 A; C/I=1-1342.
DR PDB; 5UAJ; X-ray; 3.92 A; C/I=1-1342.
DR PDB; 5UAL; X-ray; 3.89 A; C/I=1-1342.
DR PDB; 5UAQ; X-ray; 3.60 A; C/I=1-1342.
DR PDB; 5VSW; X-ray; 4.29 A; C/I=1-1342.
DR PDB; 5VT0; EM; 3.78 A; I=1-1342.
DR PDB; 5W1S; X-ray; 3.81 A; C/I=1-1342.
DR PDB; 5W1T; X-ray; 4.50 A; C/I=1-1342.
DR PDB; 6ALF; EM; 4.10 A; I=1-1342.
DR PDB; 6ALG; EM; 3.70 A; I=1-1342.
DR PDB; 6ALH; EM; 4.40 A; I=1-1342.
DR PDB; 6ASX; EM; 3.80 A; I=1-1342.
DR PDB; 6BJS; EM; 5.50 A; I=1-1342.
DR PDB; 6BYU; X-ray; 3.60 A; C/I=1-1342.
DR PDB; 6C6S; EM; 3.70 A; I=1-1342.
DR PDB; 6C6T; EM; 3.50 A; I=1-1342.
DR PDB; 6C6U; EM; 3.70 A; I=1-1342.
DR PDB; 6C9Y; EM; 4.25 A; C=1-1342.
DR PDB; 6CA0; EM; 5.75 A; C=1-1342.
DR PDB; 6CUX; X-ray; 4.10 A; C/I=1-1342.
DR PDB; 6FLP; EM; 4.10 A; C=1-1342.
DR PDB; 6FLQ; EM; 4.10 A; C=1-1342.
DR PDB; 6GFW; EM; 3.70 A; C=1-1342.
DR PDB; 6GH5; EM; 3.40 A; C=1-1342.
DR PDB; 6GH6; EM; 4.10 A; C=1-1342.
DR PDB; 6JBQ; EM; 4.02 A; C=1-1342.
DR PDB; 6JNX; EM; 4.08 A; C=1-1342.
DR PDB; 6K4Y; EM; 3.79 A; C=1-1342.
DR PDB; 6KJ6; EM; 3.80 A; C=1-1342.
DR PDB; 6LDI; EM; 3.69 A; C=1-1342.
DR PDB; 6N4C; EM; 17.00 A; C=2-1342.
DR PDB; 6N57; EM; 3.70 A; I=1-1342.
DR PDB; 6N58; EM; 3.78 A; I=1-1342.
DR PDB; 6N60; X-ray; 3.68 A; C=1-1342.
DR PDB; 6N61; X-ray; 3.25 A; C=1-1342.
DR PDB; 6OMF; EM; 3.26 A; C=1-1342.
DR PDB; 6OUL; EM; 3.40 A; I=1-1342.
DR PDB; 6P18; EM; 3.50 A; C=1-1342.
DR PDB; 6P19; EM; 3.80 A; C=1-1342.
DR PDB; 6P1K; EM; 4.05 A; I=1-1342.
DR PDB; 6PSQ; EM; 3.40 A; I=1-1342.
DR PDB; 6PSR; EM; 3.40 A; I=1-1342.
DR PDB; 6PSS; EM; 3.50 A; I=1-1342.
DR PDB; 6PST; EM; 3.00 A; I=1-1342.
DR PDB; 6PSU; EM; 3.90 A; I=1-1342.
DR PDB; 6PSV; EM; 3.50 A; I=1-1342.
DR PDB; 6PSW; EM; 3.70 A; I=1-1342.
DR PDB; 6R9B; EM; 3.80 A; C=1-1342.
DR PDB; 6R9G; EM; 3.70 A; C=1-1342.
DR PDB; 6RH3; EM; 3.60 A; C=1-1342.
DR PDB; 6RI7; EM; 3.90 A; C=1-1342.
DR PDB; 6RI9; EM; 3.70 A; C=1-1342.
DR PDB; 6RIN; EM; 3.70 A; C=1-1342.
DR PDB; 6RIP; EM; 3.40 A; C=1-1342.
DR PDB; 6TQN; EM; 3.80 A; X=1-1342.
DR PDB; 6TQO; EM; 4.00 A; X=1-1342.
DR PDB; 6UTV; X-ray; 3.45 A; CCC=1-1342.
DR PDB; 6VJS; X-ray; 4.02 A; C/H=1-1342.
DR PDB; 6WMU; EM; 3.18 A; C=1-1342.
DR PDB; 6X26; EM; 4.10 A; I=1-1342.
DR PDB; 6X2F; EM; 4.00 A; I=1-1342.
DR PDB; 6X2N; EM; 3.90 A; I=1-1342.
DR PDB; 6X43; EM; 3.60 A; I=1-1342.
DR PDB; 6X4W; EM; 3.80 A; I=1-1342.
DR PDB; 6X4Y; EM; 3.60 A; I=1-1342.
DR PDB; 6X50; EM; 3.30 A; I=1-1342.
DR PDB; 6XAS; EM; 3.80 A; I=1-1342.
DR PDB; 6XAV; EM; 7.70 A; I=1-1342.
DR PDB; 6XH7; EM; 3.90 A; C=1-1342.
DR PDB; 6XH8; EM; 4.10 A; C=1-1342.
DR PDB; 6XL5; EM; 2.50 A; C=1-1342.
DR PDB; 6XL9; EM; 2.50 A; C=1-1342.
DR PDB; 6XLJ; EM; 2.70 A; C=1-1342.
DR PDB; 6XLL; EM; 2.70 A; C=1-1342.
DR PDB; 6XLM; EM; 3.20 A; C=1-1342.
DR PDB; 6XLN; EM; 2.80 A; C=1-1342.
DR PDB; 6Z9P; EM; 3.90 A; X=1-1342.
DR PDB; 6Z9Q; EM; 5.70 A; X=1-1342.
DR PDB; 6Z9R; EM; 4.10 A; X=1-1342.
DR PDB; 6Z9S; EM; 4.40 A; X=1-1342.
DR PDB; 6Z9T; EM; 4.10 A; X=1-1342.
DR PDB; 6ZTL; EM; 3.50 A; CC=1-1342.
DR PDB; 7ADB; EM; 4.40 A; X=1-1342.
DR PDB; 7ADC; EM; 4.00 A; X=1-1342.
DR PDB; 7ADD; EM; 4.30 A; X=1-1342.
DR PDB; 7ADE; EM; 4.20 A; X=1-1342.
DR PDB; 7BEF; EM; 4.50 A; C=1-1342.
DR PDB; 7C17; EM; 4.22 A; C=1-1342.
DR PDB; 7C97; EM; 3.68 A; C=1-1342.
DR PDB; 7CHW; EM; 3.58 A; C=1-1342.
DR PDB; 7DY6; EM; 3.68 A; C=1-1342.
DR PDB; 7EGS; X-ray; 1.70 A; A=152-443.
DR PDB; 7KHB; EM; 3.53 A; C=1-1342.
DR PDB; 7KHC; EM; 4.14 A; C=1-1342.
DR PDB; 7KHE; EM; 3.58 A; C=1-1342.
DR PDB; 7KHI; EM; 3.62 A; C=1-1342.
DR PDB; 7M8E; EM; 3.40 A; C=1-1342.
DR PDB; 7MKD; EM; 3.20 A; I=1-1342.
DR PDB; 7MKE; EM; 3.70 A; I=1-1342.
DR PDB; 7MKI; EM; 3.50 A; I=1-1342.
DR PDB; 7MKJ; EM; 2.90 A; I=1-1342.
DR PDB; 7MKN; EM; 3.30 A; C=3-1342.
DR PDB; 7MKO; EM; 3.15 A; C=3-1342.
DR PDB; 7MKP; EM; 3.41 A; C=3-1342.
DR PDB; 7MKQ; EM; 4.80 A; C=3-1342.
DR PDBsum; 3IYD; -.
DR PDBsum; 3LTI; -.
DR PDBsum; 3LU0; -.
DR PDBsum; 3T72; -.
DR PDBsum; 3TBI; -.
DR PDBsum; 4JK1; -.
DR PDBsum; 4JK2; -.
DR PDBsum; 4KMU; -.
DR PDBsum; 4KN4; -.
DR PDBsum; 4KN7; -.
DR PDBsum; 4MEX; -.
DR PDBsum; 4MEY; -.
DR PDBsum; 4S20; -.
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; 6OUL; -.
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; 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; 6ZTL; -.
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; 7EGS; -.
DR PDBsum; 7KHB; -.
DR PDBsum; 7KHC; -.
DR PDBsum; 7KHE; -.
DR PDBsum; 7KHI; -.
DR PDBsum; 7M8E; -.
DR PDBsum; 7MKD; -.
DR PDBsum; 7MKE; -.
DR PDBsum; 7MKI; -.
DR PDBsum; 7MKJ; -.
DR PDBsum; 7MKN; -.
DR PDBsum; 7MKO; -.
DR PDBsum; 7MKP; -.
DR PDBsum; 7MKQ; -.
DR AlphaFoldDB; P0A8V2; -.
DR SMR; P0A8V2; -.
DR BioGRID; 4263472; 52.
DR BioGRID; 852782; 2.
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-35777N; -.
DR IntAct; P0A8V2; 103.
DR STRING; 511145.b3987; -.
DR BindingDB; P0A8V2; -.
DR ChEMBL; CHEMBL1852; -.
DR DrugBank; DB00615; Rifabutin.
DR DrugBank; DB04934; Rifalazil.
DR DrugBank; DB01045; Rifampicin.
DR DrugBank; DB11753; Rifamycin.
DR DrugBank; DB01220; Rifaximin.
DR DrugCentral; P0A8V2; -.
DR CarbonylDB; P0A8V2; -.
DR iPTMnet; P0A8V2; -.
DR SWISS-2DPAGE; P0A8V2; -.
DR jPOST; P0A8V2; -.
DR PaxDb; P0A8V2; -.
DR PRIDE; P0A8V2; -.
DR EnsemblBacteria; AAC76961; AAC76961; b3987.
DR EnsemblBacteria; BAE77333; BAE77333; BAE77333.
DR GeneID; 67415312; -.
DR GeneID; 948488; -.
DR KEGG; ecj:JW3950; -.
DR KEGG; eco:b3987; -.
DR PATRIC; fig|1411691.4.peg.2725; -.
DR EchoBASE; EB0887; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_6; -.
DR InParanoid; P0A8V2; -.
DR OMA; FMTWEGY; -.
DR PhylomeDB; P0A8V2; -.
DR BioCyc; EcoCyc:RPOB-MON; -.
DR BioCyc; MetaCyc:RPOB-MON; -.
DR BRENDA; 2.7.7.6; 2026.
DR EvolutionaryTrace; P0A8V2; -.
DR PRO; PR:P0A8V2; -.
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:0032549; F:ribonucleoside binding; IEA:InterPro.
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 CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.30.150.10; -; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR InterPro; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf.
DR InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR010243; RNA_pol_bsu_bac.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 2.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF10385; RNA_pol_Rpb2_45; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR TIGRFAMs; TIGR02013; rpoB; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Antibiotic resistance;
KW Direct protein sequencing; DNA-directed RNA polymerase;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase.
FT CHAIN 1..1342
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047892"
FT MOD_RES 1022
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 1200
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MUTAGEN 561
FT /note="I->S: Resistant to antibiotics salinamide A and B."
FT /evidence="ECO:0000269|PubMed:24843001"
FT MUTAGEN 569
FT /note="I->S: Resistant to antibiotics salinamide A and B."
FT /evidence="ECO:0000269|PubMed:24843001"
FT MUTAGEN 665
FT /note="A->E: Resistant to antibiotics salinamide A and B."
FT /evidence="ECO:0000269|PubMed:24843001"
FT MUTAGEN 675
FT /note="D->A,G: Resistant to antibiotics salinamide A and
FT B."
FT /evidence="ECO:0000269|PubMed:24843001"
FT MUTAGEN 677
FT /note="N->H,K: Resistant to antibiotics salinamide A and
FT B."
FT /evidence="ECO:0000269|PubMed:24843001"
FT MUTAGEN 680
FT /note="L->M: Resistant to antibiotics salinamide A and B."
FT /evidence="ECO:0000269|PubMed:24843001"
FT MUTAGEN 813
FT /note="E->K: Disrupts the enzyme's active center."
FT /evidence="ECO:0000269|PubMed:2068078"
FT CONFLICT 4
FT /note="S -> R (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 106..107
FT /note="ER -> G (in Ref. 6; CAA23629)"
FT /evidence="ECO:0000305"
FT CONFLICT 384..391
FT /note="LFENLFFS -> CSRTCSSPT (in Ref. 6; CAA23629)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="D -> V (in Ref. 1; CAA23625/CAA23627 and 11;
FT AAA24585)"
FT /evidence="ECO:0000305"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 62..75
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 93..105
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:6XL9"
FT STRAND 114..128
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:6X50"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:3LTI"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:7MKN"
FT TURN 165..168
FT /evidence="ECO:0007829|PDB:6XLJ"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:3LTI"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:3LTI"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:3LTI"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:6PSR"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:3LTI"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:6PSV"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:6PSR"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:3LTI"
FT HELIX 217..224
FT /evidence="ECO:0007829|PDB:3LTI"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:3LTI"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:3LTI"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:3LTI"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:3LTI"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:3LTI"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:6XLL"
FT HELIX 271..279
FT /evidence="ECO:0007829|PDB:3LTI"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:3LTI"
FT HELIX 289..293
FT /evidence="ECO:0007829|PDB:3LTI"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:6XLN"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:6XLL"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:3LTI"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:3LTI"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:6WMU"
FT HELIX 319..323
FT /evidence="ECO:0007829|PDB:3LTI"
FT TURN 326..329
FT /evidence="ECO:0007829|PDB:3LTI"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:3LTI"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:3LTI"
FT HELIX 346..353
FT /evidence="ECO:0007829|PDB:3LTI"
FT HELIX 359..370
FT /evidence="ECO:0007829|PDB:3LTI"
FT STRAND 371..374
FT /evidence="ECO:0007829|PDB:6X50"
FT HELIX 378..389
FT /evidence="ECO:0007829|PDB:3LTI"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:3LTI"
FT HELIX 398..403
FT /evidence="ECO:0007829|PDB:3LTI"
FT TURN 406..410
FT /evidence="ECO:0007829|PDB:3LTI"
FT HELIX 424..429
FT /evidence="ECO:0007829|PDB:3LTI"
FT HELIX 433..437
FT /evidence="ECO:0007829|PDB:3LTI"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:6PSV"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:6XL9"
FT STRAND 450..454
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 456..479
FT /evidence="ECO:0007829|PDB:6XL5"
FT TURN 484..486
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 495..508
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 510..514
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 520..527
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 529..534
FT /evidence="ECO:0007829|PDB:6XL5"
FT TURN 540..542
FT /evidence="ECO:0007829|PDB:6XL5"
FT TURN 545..548
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 552..554
FT /evidence="ECO:0007829|PDB:6XL5"
FT TURN 555..557
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 565..578
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 583..585
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 587..607
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 608..611
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 612..614
FT /evidence="ECO:0007829|PDB:6XLL"
FT STRAND 619..622
FT /evidence="ECO:0007829|PDB:6N61"
FT STRAND 627..646
FT /evidence="ECO:0007829|PDB:6XL5"
FT TURN 647..649
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 652..655
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 657..662
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 665..667
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 671..673
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 676..686
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 692..694
FT /evidence="ECO:0007829|PDB:6XLN"
FT STRAND 699..701
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 705..711
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 715..717
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 722..728
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 731..736
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 738..740
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 743..745
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 748..752
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 756..758
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 762..765
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 782..785
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 789..794
FT /evidence="ECO:0007829|PDB:6XL9"
FT STRAND 797..805
FT /evidence="ECO:0007829|PDB:6XL5"
FT TURN 808..811
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 812..814
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 815..819
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 820..824
FT /evidence="ECO:0007829|PDB:6XL5"
FT TURN 825..828
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 830..843
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 849..852
FT /evidence="ECO:0007829|PDB:3TBI"
FT STRAND 855..857
FT /evidence="ECO:0007829|PDB:6XLN"
FT TURN 859..864
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 869..871
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 876..878
FT /evidence="ECO:0007829|PDB:6XL9"
FT STRAND 882..884
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 886..889
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 892..894
FT /evidence="ECO:0007829|PDB:3TBI"
FT HELIX 897..906
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 907..910
FT /evidence="ECO:0007829|PDB:6GH5"
FT STRAND 912..915
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 926..935
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 937..939
FT /evidence="ECO:0007829|PDB:6N61"
FT HELIX 943..981
FT /evidence="ECO:0007829|PDB:6XL5"
FT TURN 986..991
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 995..999
FT /evidence="ECO:0007829|PDB:6XL5"
FT TURN 1004..1006
FT /evidence="ECO:0007829|PDB:6XLN"
FT HELIX 1007..1037
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 1046..1058
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 1065..1067
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 1069..1071
FT /evidence="ECO:0007829|PDB:6XLL"
FT STRAND 1074..1080
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 1082..1084
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 1095..1098
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 1102..1105
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 1110..1133
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 1138..1150
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 1152..1154
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 1161..1163
FT /evidence="ECO:0007829|PDB:6XL9"
FT HELIX 1166..1175
FT /evidence="ECO:0007829|PDB:6XL5"
FT TURN 1176..1178
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 1186..1188
FT /evidence="ECO:0007829|PDB:6XL9"
FT HELIX 1192..1201
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 1202..1204
FT /evidence="ECO:0007829|PDB:6X50"
FT STRAND 1208..1210
FT /evidence="ECO:0007829|PDB:6XL5"
FT TURN 1215..1217
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 1225..1236
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 1239..1242
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 1244..1248
FT /evidence="ECO:0007829|PDB:6XL9"
FT STRAND 1251..1255
FT /evidence="ECO:0007829|PDB:6XL5"
FT TURN 1262..1265
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 1268..1270
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 1272..1280
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 1284..1291
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 1292..1296
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 1298..1309
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 1321..1330
FT /evidence="ECO:0007829|PDB:6XL5"
FT TURN 1331..1334
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 1335..1340
FT /evidence="ECO:0007829|PDB:6XL5"
SQ SEQUENCE 1342 AA; 150632 MW; F9E95344C54AB118 CRC64;
MVYSYTEKKR IRKDFGKRPQ VLDVPYLLSI QLDSFQKFIE QDPEGQYGLE AAFRSVFPIQ
SYSGNSELQY VSYRLGEPVF DVQECQIRGV TYSAPLRVKL RLVIYEREAP EGTVKDIKEQ
EVYMGEIPLM TDNGTFVING TERVIVSQLH RSPGVFFDSD KGKTHSSGKV LYNARIIPYR
GSWLDFEFDP KDNLFVRIDR RRKLPATIIL RALNYTTEQI LDLFFEKVIF EIRDNKLQME
LVPERLRGET ASFDIEANGK VYVEKGRRIT ARHIRQLEKD DVKLIEVPVE YIAGKVVAKD
YIDESTGELI CAANMELSLD LLAKLSQSGH KRIETLFTND LDHGPYISET LRVDPTNDRL
SALVEIYRMM RPGEPPTREA AESLFENLFF SEDRYDLSAV GRMKFNRSLL REEIEGSGIL
SKDDIIDVMK KLIDIRNGKG EVDDIDHLGN RRIRSVGEMA ENQFRVGLVR VERAVKERLS
LGDLDTLMPQ DMINAKPISA AVKEFFGSSQ LSQFMDQNNP LSEITHKRRI SALGPGGLTR
ERAGFEVRDV HPTHYGRVCP IETPEGPNIG LINSLSVYAQ TNEYGFLETP YRKVTDGVVT
DEIHYLSAIE EGNYVIAQAN SNLDEEGHFV EDLVTCRSKG ESSLFSRDQV DYMDVSTQQV
VSVGASLIPF LEHDDANRAL MGANMQRQAV PTLRADKPLV GTGMERAVAV DSGVTAVAKR
GGVVQYVDAS RIVIKVNEDE MYPGEAGIDI YNLTKYTRSN QNTCINQMPC VSLGEPVERG
DVLADGPSTD LGELALGQNM RVAFMPWNGY NFEDSILVSE RVVQEDRFTT IHIQELACVS
RDTKLGPEEI TADIPNVGEA ALSKLDESGI VYIGAEVTGG DILVGKVTPK GETQLTPEEK
LLRAIFGEKA SDVKDSSLRV PNGVSGTVID VQVFTRDGVE KDKRALEIEE MQLKQAKKDL
SEELQILEAG LFSRIRAVLV AGGVEAEKLD KLPRDRWLEL GLTDEEKQNQ LEQLAEQYDE
LKHEFEKKLE AKRRKITQGD DLAPGVLKIV KVYLAVKRRI QPGDKMAGRH GNKGVISKIN
PIEDMPYDEN GTPVDIVLNP LGVPSRMNIG QILETHLGMA AKGIGDKINA MLKQQQEVAK
LREFIQRAYD LGADVRQKVD LSTFSDEEVM RLAENLRKGM PIATPVFDGA KEAEIKELLK
LGDLPTSGQI RLYDGRTGEQ FERPVTVGYM YMLKLNHLVD DKMHARSTGS YSLVTQQPLG
GKAQFGGQRF GEMEVWALEA YGAAYTLQEM LTVKSDDVNG RTKMYKNIVD GNHQMEPGMP
ESFNVLLKEI RSLGINIELE DE
