RPOZ_ECOLI
ID RPOZ_ECOLI Reviewed; 91 AA.
AC P0A800; P08374; Q2M7W2;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=DNA-directed RNA polymerase subunit omega;
DE Short=RNAP omega subunit;
DE EC=2.7.7.6;
DE AltName: Full=RNA polymerase omega subunit;
DE AltName: Full=Transcriptase subunit omega;
GN Name=rpoZ; OrderedLocusNames=b3649, JW3624;
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=3549461; DOI=10.1016/0378-1119(86)90349-5;
RA Gentry D.R., Burgess R.R.;
RT "The cloning and sequence of the gene encoding the omega subunit of
RT Escherichia coli RNA polymerase.";
RL Gene 48:33-40(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=2549050; DOI=10.1016/s0021-9258(18)63813-x;
RA Sarubbi E., Rudd K.E., Xiao H., Ikehara K., Kalman M., Cashel M.;
RT "Characterization of the spoT gene of Escherichia coli.";
RL J. Biol. Chem. 264:15074-15082(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(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 PROTEIN SEQUENCE OF 2-11.
RC STRAIN=K12;
RX PubMed=9868784; DOI=10.1111/j.1574-6968.1998.tb13343.x;
RA Wasinger V.C., Humphery-Smith I.;
RT "Small genes/gene-products in Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 169:375-382(1998).
RN [7] {ECO:0007744|PDB:3IYD}
RP STRUCTURE BY ELECTRON MICROSCOPY (19.80 ANGSTROMS) IN COMPLEX WITH RPOA;
RP RPOB; RPOC; RPOD; 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 [8] {ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY}
RP X-RAY CRYSTALLOGRAPHY (3.90 ANGSTROMS) IN COMPLEX WITH RPOA; RPOB; RPOC;
RP RPOD AND SALINAMIDE A, FUNCTION, AND SUBUNIT.
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 [9] {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: Promotes RNA polymerase (RNAP) assembly. Latches the N- and
CC C-terminal regions of the beta' subunit thereby facilitating its
CC interaction with the beta and alpha subunits.
CC {ECO:0000269|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:19903881,
CC ECO:0000269|PubMed:24843001, ECO:0000269|PubMed:32871103}.
CC -!- SIMILARITY: Belongs to the RNA polymerase subunit omega family.
CC {ECO:0000305}.
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DR EMBL; M24503; AAB00159.1; -; Genomic_DNA.
DR EMBL; M15266; AAA24229.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62002.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76673.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77644.1; -; Genomic_DNA.
DR PIR; A29038; RNECO.
DR RefSeq; NP_418106.1; NC_000913.3.
DR RefSeq; WP_000135058.1; NZ_STEB01000024.1.
DR PDB; 3IYD; EM; -; E=2-91.
DR PDB; 3LU0; EM; -; E=1-91.
DR PDB; 4JK1; X-ray; 3.90 A; E/J=1-91.
DR PDB; 4JK2; X-ray; 4.20 A; E/J=1-91.
DR PDB; 4KMU; X-ray; 3.85 A; E/J=1-91.
DR PDB; 4KN4; X-ray; 3.96 A; E/J=1-91.
DR PDB; 4KN7; X-ray; 3.69 A; E/J=1-91.
DR PDB; 4MEX; X-ray; 3.90 A; E/K=1-91.
DR PDB; 4MEY; X-ray; 3.95 A; E/K=1-91.
DR PDB; 4XSX; X-ray; 3.71 A; E/K=1-91.
DR PDB; 4XSY; X-ray; 4.01 A; E/K=1-91.
DR PDB; 4XSZ; X-ray; 3.68 A; E/K=1-91.
DR PDB; 4YG2; X-ray; 3.70 A; E/K=1-91.
DR PDB; 4YLN; X-ray; 5.50 A; E/K/Q=2-91.
DR PDB; 4YLO; X-ray; 6.00 A; E/K/Q=2-91.
DR PDB; 4YLP; X-ray; 5.50 A; E/K/Q=2-91.
DR PDB; 4ZH2; X-ray; 4.20 A; E/K=1-91.
DR PDB; 4ZH3; X-ray; 4.08 A; E/K=1-91.
DR PDB; 4ZH4; X-ray; 3.99 A; E/K=1-91.
DR PDB; 5BYH; X-ray; 3.76 A; E=1-91.
DR PDB; 5EZK; X-ray; 8.50 A; E=1-91.
DR PDB; 5IPL; X-ray; 3.60 A; E=2-91.
DR PDB; 5IPM; X-ray; 4.20 A; E=2-91.
DR PDB; 5IPN; X-ray; 4.61 A; E=2-91.
DR PDB; 5MS0; EM; 9.80 A; O=1-91.
DR PDB; 5MY1; EM; 7.60 A; Z=1-91.
DR PDB; 5NSR; EM; 3.80 A; E=1-91.
DR PDB; 5NSS; EM; 5.80 A; E=1-91.
DR PDB; 5NWT; X-ray; 3.76 A; E=1-91.
DR PDB; 5UAC; X-ray; 3.80 A; E/K=1-91.
DR PDB; 5UAG; X-ray; 3.40 A; E/K=2-91.
DR PDB; 5UAH; X-ray; 4.10 A; E/K=1-91.
DR PDB; 5UAJ; X-ray; 3.92 A; E/K=1-91.
DR PDB; 5UAL; X-ray; 3.89 A; E/K=1-91.
DR PDB; 5UAQ; X-ray; 3.60 A; E/K=1-91.
DR PDB; 5VSW; X-ray; 4.29 A; E/K=1-91.
DR PDB; 5VT0; EM; 3.78 A; K=1-91.
DR PDB; 5W1S; X-ray; 3.81 A; E/K=1-91.
DR PDB; 5W1T; X-ray; 4.50 A; E/K=1-91.
DR PDB; 6ALF; EM; 4.10 A; K=1-80.
DR PDB; 6ALG; EM; 3.74 A; K=1-91.
DR PDB; 6ALH; EM; 4.40 A; K=1-80.
DR PDB; 6ASX; EM; 3.80 A; K=1-84.
DR PDB; 6BJS; EM; 5.50 A; K=1-91.
DR PDB; 6BYU; X-ray; 3.60 A; E/K=1-91.
DR PDB; 6C6S; EM; 3.70 A; K=1-91.
DR PDB; 6C6T; EM; 3.50 A; K=1-91.
DR PDB; 6C6U; EM; 3.70 A; K=1-91.
DR PDB; 6C9Y; EM; 4.25 A; E=1-91.
DR PDB; 6CA0; EM; 5.75 A; E=1-91.
DR PDB; 6CUX; X-ray; 4.10 A; E/K=1-91.
DR PDB; 6FLP; EM; 4.10 A; E=1-91.
DR PDB; 6FLQ; EM; 4.10 A; E=1-91.
DR PDB; 6GFW; EM; 3.70 A; E=1-91.
DR PDB; 6GH5; EM; 3.40 A; E=1-91.
DR PDB; 6GH6; EM; 4.10 A; E=1-91.
DR PDB; 6JBQ; EM; 4.02 A; E=1-91.
DR PDB; 6JNX; EM; 4.08 A; E=1-91.
DR PDB; 6K4Y; EM; 3.79 A; E=1-91.
DR PDB; 6KJ6; EM; 3.80 A; E=1-91.
DR PDB; 6LDI; EM; 3.69 A; E=1-91.
DR PDB; 6N4C; EM; 17.00 A; E=2-91.
DR PDB; 6N57; EM; 3.70 A; K=1-91.
DR PDB; 6N58; EM; 3.78 A; K=1-91.
DR PDB; 6N60; X-ray; 3.68 A; E=1-91.
DR PDB; 6N61; X-ray; 3.25 A; E=1-90.
DR PDB; 6OMF; EM; 3.26 A; E=1-91.
DR PDB; 6OUL; EM; 3.40 A; K=1-91.
DR PDB; 6P18; EM; 3.50 A; E=1-91.
DR PDB; 6P19; EM; 3.80 A; E=1-91.
DR PDB; 6P1K; EM; 4.05 A; K=1-91.
DR PDB; 6PB4; EM; 4.35 A; E=1-91.
DR PDB; 6PB5; EM; 4.52 A; E=1-91.
DR PDB; 6PB6; EM; 4.29 A; E=1-91.
DR PDB; 6PMI; EM; 3.86 A; E=1-91.
DR PDB; 6PMJ; EM; 3.91 A; E=1-91.
DR PDB; 6PSQ; EM; 3.40 A; K=1-91.
DR PDB; 6PSR; EM; 3.40 A; K=1-91.
DR PDB; 6PSS; EM; 3.50 A; K=1-91.
DR PDB; 6PST; EM; 3.00 A; K=1-91.
DR PDB; 6PSU; EM; 3.90 A; K=1-91.
DR PDB; 6PSV; EM; 3.50 A; K=1-91.
DR PDB; 6PSW; EM; 3.70 A; K=1-91.
DR PDB; 6R9B; EM; 3.80 A; E=1-80.
DR PDB; 6R9G; EM; 3.70 A; E=1-80.
DR PDB; 6RI7; EM; 3.90 A; E=1-91.
DR PDB; 6RI9; EM; 3.70 A; E=1-91.
DR PDB; 6RIN; EM; 3.70 A; E=1-91.
DR PDB; 6RIP; EM; 3.40 A; E=1-91.
DR PDB; 6TQN; EM; 3.80 A; W=1-91.
DR PDB; 6TQO; EM; 3.80 A; W=1-91.
DR PDB; 6UTV; X-ray; 3.45 A; EEE=2-91.
DR PDB; 6UTW; X-ray; 3.85 A; EEE=2-91.
DR PDB; 6UTX; X-ray; 4.05 A; EEE=2-91.
DR PDB; 6UTY; X-ray; 4.15 A; EEE=2-91.
DR PDB; 6UTZ; X-ray; 3.80 A; EEE=2-91.
DR PDB; 6UU0; X-ray; 3.90 A; EEE=2-91.
DR PDB; 6UU1; X-ray; 4.10 A; EEE=2-91.
DR PDB; 6UU2; X-ray; 4.40 A; EEE=2-91.
DR PDB; 6UU3; X-ray; 4.00 A; EEE=2-91.
DR PDB; 6UU4; X-ray; 4.30 A; EEE=2-91.
DR PDB; 6UU5; X-ray; 5.40 A; EEE=2-91.
DR PDB; 6UU6; X-ray; 4.20 A; EEE=2-91.
DR PDB; 6UU7; X-ray; 4.40 A; EEE=2-91.
DR PDB; 6UU8; X-ray; 4.40 A; EEE=2-91.
DR PDB; 6UU9; X-ray; 5.40 A; EEE=2-91.
DR PDB; 6UUA; X-ray; 4.00 A; EEE=2-91.
DR PDB; 6UUB; X-ray; 3.96 A; EEE=2-91.
DR PDB; 6UUC; X-ray; 4.10 A; EEE=2-91.
DR PDB; 6VJS; X-ray; 4.02 A; E/J=1-91.
DR PDB; 6WMU; EM; 3.18 A; E=1-91.
DR PDB; 6X26; EM; 4.10 A; K=1-91.
DR PDB; 6X2F; EM; 4.00 A; K=1-91.
DR PDB; 6X2N; EM; 3.90 A; K=1-91.
DR PDB; 6X43; EM; 3.60 A; K=1-91.
DR PDB; 6X4W; EM; 3.80 A; K=1-91.
DR PDB; 6X4Y; EM; 3.60 A; K=1-91.
DR PDB; 6X50; EM; 3.30 A; K=1-91.
DR PDB; 6XAS; EM; 3.80 A; W=1-91.
DR PDB; 6XAV; EM; 7.70 A; W=1-91.
DR PDB; 6XH7; EM; 3.90 A; E=1-91.
DR PDB; 6XH8; EM; 4.10 A; E=1-91.
DR PDB; 6XL5; EM; 2.50 A; E=1-91.
DR PDB; 6XLJ; EM; 2.70 A; E=1-91.
DR PDB; 6XLL; EM; 2.70 A; E=1-91.
DR PDB; 6XLM; EM; 3.20 A; E=1-91.
DR PDB; 6XLN; EM; 2.80 A; E=1-91.
DR PDB; 6Z9P; EM; 3.90 A; W=1-91.
DR PDB; 6Z9Q; EM; 5.70 A; W=1-91.
DR PDB; 6Z9R; EM; 4.10 A; W=1-91.
DR PDB; 6Z9S; EM; 4.40 A; W=1-91.
DR PDB; 6Z9T; EM; 4.10 A; W=1-91.
DR PDB; 6ZTJ; EM; 3.40 A; CE=1-91.
DR PDB; 6ZTL; EM; 3.50 A; CE=1-91.
DR PDB; 6ZTN; EM; 3.90 A; CE=1-91.
DR PDB; 6ZTO; EM; 3.00 A; CE=1-91.
DR PDB; 6ZTP; EM; 3.00 A; CE=1-91.
DR PDB; 6ZU1; EM; 3.00 A; CE=1-91.
DR PDB; 7ADB; EM; 4.40 A; W=1-91.
DR PDB; 7ADC; EM; 4.00 A; W=1-91.
DR PDB; 7ADD; EM; 4.30 A; W=1-91.
DR PDB; 7ADE; EM; 4.20 A; W=1-91.
DR PDB; 7BEF; EM; 4.50 A; E=1-91.
DR PDB; 7BEG; EM; 4.20 A; E=1-91.
DR PDB; 7C17; EM; 4.22 A; E=1-91.
DR PDB; 7C97; EM; 3.68 A; E=1-91.
DR PDB; 7CHW; EM; 3.58 A; E=1-91.
DR PDB; 7KHB; EM; 3.53 A; E=1-91.
DR PDB; 7KHC; EM; 4.14 A; E=1-91.
DR PDB; 7KHE; EM; 3.58 A; E=1-91.
DR PDB; 7KHI; EM; 3.62 A; E=1-91.
DR PDB; 7M8E; EM; 3.40 A; E=1-91.
DR PDB; 7MKD; EM; 3.20 A; K=1-91.
DR PDB; 7MKE; EM; 3.70 A; K=1-91.
DR PDB; 7MKI; EM; 3.50 A; K=1-91.
DR PDB; 7MKJ; EM; 2.90 A; K=1-91.
DR PDB; 7MKN; EM; 3.30 A; E=1-91.
DR PDB; 7MKO; EM; 3.15 A; E=1-91.
DR PDB; 7MKP; EM; 3.41 A; E=1-91.
DR PDB; 7MKQ; EM; 4.80 A; E=1-91.
DR PDB; 7PY0; EM; 4.50 A; E=1-91.
DR PDB; 7PY1; EM; 3.80 A; E=1-91.
DR PDB; 7PY3; EM; 3.80 A; E=1-91.
DR PDB; 7PY5; EM; 3.90 A; E=1-91.
DR PDB; 7PY6; EM; 4.10 A; E=1-91.
DR PDB; 7PY7; EM; 4.10 A; E=1-91.
DR PDB; 7PY8; EM; 3.80 A; E=1-91.
DR PDB; 7PYJ; EM; 4.20 A; E=1-91.
DR PDB; 7PYK; EM; 4.10 A; E=1-91.
DR PDB; 7Q0J; EM; 4.30 A; E=1-91.
DR PDB; 7Q0K; EM; 4.00 A; E=1-91.
DR PDBsum; 3IYD; -.
DR PDBsum; 3LU0; -.
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; 6OUL; -.
DR PDBsum; 6P18; -.
DR PDBsum; 6P19; -.
DR PDBsum; 6P1K; -.
DR PDBsum; 6PB4; -.
DR PDBsum; 6PB5; -.
DR PDBsum; 6PB6; -.
DR PDBsum; 6PMI; -.
DR PDBsum; 6PMJ; -.
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; 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; 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; 6ZTJ; -.
DR PDBsum; 6ZTL; -.
DR PDBsum; 6ZTN; -.
DR PDBsum; 6ZTO; -.
DR PDBsum; 6ZTP; -.
DR PDBsum; 6ZU1; -.
DR PDBsum; 7ADB; -.
DR PDBsum; 7ADC; -.
DR PDBsum; 7ADD; -.
DR PDBsum; 7ADE; -.
DR PDBsum; 7BEF; -.
DR PDBsum; 7BEG; -.
DR PDBsum; 7C17; -.
DR PDBsum; 7C97; -.
DR PDBsum; 7CHW; -.
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 PDBsum; 7PY0; -.
DR PDBsum; 7PY1; -.
DR PDBsum; 7PY3; -.
DR PDBsum; 7PY5; -.
DR PDBsum; 7PY6; -.
DR PDBsum; 7PY7; -.
DR PDBsum; 7PY8; -.
DR PDBsum; 7PYJ; -.
DR PDBsum; 7PYK; -.
DR PDBsum; 7Q0J; -.
DR PDBsum; 7Q0K; -.
DR AlphaFoldDB; P0A800; -.
DR SMR; P0A800; -.
DR BioGRID; 4259347; 290.
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-31837N; -.
DR IntAct; P0A800; 27.
DR STRING; 511145.b3649; -.
DR BindingDB; P0A800; -.
DR ChEMBL; CHEMBL2364672; -.
DR ChEMBL; CHEMBL4296169; -.
DR DrugCentral; P0A800; -.
DR jPOST; P0A800; -.
DR PaxDb; P0A800; -.
DR PRIDE; P0A800; -.
DR EnsemblBacteria; AAC76673; AAC76673; b3649.
DR EnsemblBacteria; BAE77644; BAE77644; BAE77644.
DR GeneID; 64726409; -.
DR GeneID; 67517126; -.
DR GeneID; 948160; -.
DR KEGG; ecj:JW3624; -.
DR KEGG; eco:b3649; -.
DR PATRIC; fig|511145.12.peg.3769; -.
DR EchoBASE; EB0892; -.
DR eggNOG; COG1758; Bacteria.
DR HOGENOM; CLU_125406_5_3_6; -.
DR InParanoid; P0A800; -.
DR OMA; NVDNRFQ; -.
DR PhylomeDB; P0A800; -.
DR BioCyc; EcoCyc:EG10899-MON; -.
DR BRENDA; 2.7.7.6; 2026.
DR EvolutionaryTrace; P0A800; -.
DR PRO; PR:P0A800; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0000345; C:cytosolic DNA-directed RNA polymerase complex; IPI:ComplexPortal.
DR GO; GO:0030880; C:RNA polymerase complex; IMP:EcoliWiki.
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: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:0065003; P:protein-containing complex assembly; IDA:EcoCyc.
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: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; 3.90.940.10; -; 1.
DR HAMAP; MF_00366; RNApol_bact_RpoZ; 1.
DR InterPro; IPR003716; DNA-dir_RNA_pol_omega.
DR InterPro; IPR006110; Pol_omega/Rpo6/RPB6.
DR InterPro; IPR036161; RPB6/omega-like_sf.
DR PANTHER; PTHR34476; PTHR34476; 1.
DR Pfam; PF01192; RNA_pol_Rpb6; 1.
DR SMART; SM01409; RNA_pol_Rpb6; 1.
DR SUPFAM; SSF63562; SSF63562; 1.
DR TIGRFAMs; TIGR00690; rpoZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-directed RNA polymerase;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9868784"
FT CHAIN 2..91
FT /note="DNA-directed RNA polymerase subunit omega"
FT /id="PRO_0000128935"
FT HELIX 7..12
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:6GH5"
FT HELIX 16..31
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:6XLJ"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:6XL5"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 61..77
FT /evidence="ECO:0007829|PDB:6XL5"
FT HELIX 80..84
FT /evidence="ECO:0007829|PDB:5UAG"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:5UAG"
SQ SEQUENCE 91 AA; 10237 MW; 4DE7E81EF670D887 CRC64;
MARVTVQDAV EKIGNRFDLV LVAARRARQM QVGGKDPLVP EENDKTTVIA LREIEEGLIN
NQILDVRERQ EQQEQEAAEL QAVTAIAEGR R
