RPOA_MYCTU
ID RPOA_MYCTU Reviewed; 347 AA.
AC P9WGZ1; L0TCT4; O06324; P66701;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=DNA-directed RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
DE Short=RNAP subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00059};
DE AltName: Full=RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
DE AltName: Full=Transcriptase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
GN Name=rpoA {ECO:0000255|HAMAP-Rule:MF_00059}; OrderedLocusNames=Rv3457c;
GN ORFNames=MTCY13E12.10c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP INDUCTION FOLLOWING STARVATION.
RC STRAIN=ATCC 25618 / H37Rv / NCTC 7416;
RX PubMed=11929527; DOI=10.1046/j.1365-2958.2002.02779.x;
RA Betts J.C., Lukey P.T., Robb L.C., McAdam R.A., Duncan K.;
RT "Evaluation of a nutrient starvation model of Mycobacterium tuberculosis
RT persistence by gene and protein expression profiling.";
RL Mol. Microbiol. 43:717-731(2002).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=22570422; DOI=10.1093/nar/gks346;
RA Hu Y., Morichaud Z., Chen S., Leonetti J.P., Brodolin K.;
RT "Mycobacterium tuberculosis RbpA protein is a new type of transcriptional
RT activator that stabilizes the sigma A-containing RNA polymerase
RT holoenzyme.";
RL Nucleic Acids Res. 40:6547-6557(2012).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_00059, ECO:0000269|PubMed:22570422}.
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_00059};
CC -!- SUBUNIT: Homodimer. The RNAP catalytic core consists of 2 alpha, 1
CC beta, 1 beta' and 1 omega subunit. When a sigma factor is associated
CC with the core the holoenzyme is formed, which can initiate
CC transcription. {ECO:0000255|HAMAP-Rule:MF_00059,
CC ECO:0000269|PubMed:22570422}.
CC -!- INDUCTION: 3-fold repressed by starvation.
CC {ECO:0000269|PubMed:11929527}.
CC -!- DOMAIN: The N-terminal domain is essential for RNAP assembly and basal
CC transcription, whereas the C-terminal domain is involved in interaction
CC with transcriptional regulators and with upstream promoter elements.
CC {ECO:0000255|HAMAP-Rule:MF_00059}.
CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00059}.
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DR EMBL; AL123456; CCP46279.1; -; Genomic_DNA.
DR PIR; F70565; F70565.
DR RefSeq; NP_217974.1; NC_000962.3.
DR RefSeq; WP_003418351.1; NZ_NVQJ01000065.1.
DR PDB; 5UH5; X-ray; 3.75 A; A/B=1-347.
DR PDB; 5UH6; X-ray; 3.84 A; A/B=1-347.
DR PDB; 5UH8; X-ray; 4.18 A; A/B=1-347.
DR PDB; 5UH9; X-ray; 4.40 A; A/B=1-347.
DR PDB; 5UHA; X-ray; 3.91 A; A/B=1-347.
DR PDB; 5UHB; X-ray; 4.29 A; A/B=1-347.
DR PDB; 5UHC; X-ray; 3.80 A; A/B=1-347.
DR PDB; 5UHD; X-ray; 4.01 A; A/B=1-347.
DR PDB; 5UHE; X-ray; 4.04 A; A/B=1-347.
DR PDB; 5UHF; X-ray; 4.34 A; A/B=1-347.
DR PDB; 5UHG; X-ray; 3.97 A; A/B=1-347.
DR PDB; 5ZX2; X-ray; 2.80 A; A/B=1-347.
DR PDB; 5ZX3; X-ray; 2.75 A; A/B=1-347.
DR PDB; 6BZO; EM; 3.38 A; A/B=1-347.
DR PDB; 6C04; EM; 3.27 A; A/B=1-347.
DR PDB; 6C05; EM; 5.15 A; A/B=1-347.
DR PDB; 6C06; EM; 5.15 A; A/B=1-347.
DR PDB; 6DV9; X-ray; 3.80 A; A/B=1-347.
DR PDB; 6DVB; X-ray; 3.80 A; A/B=1-347.
DR PDB; 6DVC; X-ray; 3.30 A; A/B=1-347.
DR PDB; 6DVD; X-ray; 3.90 A; A/B=1-347.
DR PDB; 6DVE; X-ray; 3.81 A; A/B=1-347.
DR PDB; 6EDT; EM; -; A/B=1-347.
DR PDB; 6EE8; EM; 3.92 A; A/B=1-347.
DR PDB; 6EEC; EM; 3.55 A; A/B=1-347.
DR PDB; 6FBV; EM; 3.50 A; A/B=1-347.
DR PDB; 6JCX; X-ray; 2.90 A; A/B=1-347.
DR PDB; 6JCY; X-ray; 3.11 A; A/B=1-347.
DR PDB; 6KON; X-ray; 3.00 A; A/B=1-347.
DR PDB; 6KOO; X-ray; 2.80 A; A/B=1-347.
DR PDB; 6KOP; X-ray; 3.30 A; A/B=1-347.
DR PDB; 6KOQ; X-ray; 3.35 A; A/B=1-347.
DR PDB; 6TYE; X-ray; 3.79 A; A/B=1-347.
DR PDB; 6TYF; X-ray; 3.80 A; A/B=1-347.
DR PDB; 6TYG; X-ray; 3.50 A; A/B=1-347.
DR PDB; 6VVX; EM; 3.39 A; A/B=1-347.
DR PDB; 6VVY; EM; 3.42 A; A/B=1-347.
DR PDB; 6VVZ; EM; 3.72 A; A/B=1-347.
DR PDB; 6VW0; EM; 3.59 A; A/B=1-347.
DR PDB; 7KIF; EM; 2.94 A; A/B=1-347.
DR PDB; 7KIM; EM; 3.38 A; A/B=1-347.
DR PDB; 7KIN; EM; 2.74 A; A/B=1-347.
DR PDBsum; 5UH5; -.
DR PDBsum; 5UH6; -.
DR PDBsum; 5UH8; -.
DR PDBsum; 5UH9; -.
DR PDBsum; 5UHA; -.
DR PDBsum; 5UHB; -.
DR PDBsum; 5UHC; -.
DR PDBsum; 5UHD; -.
DR PDBsum; 5UHE; -.
DR PDBsum; 5UHF; -.
DR PDBsum; 5UHG; -.
DR PDBsum; 5ZX2; -.
DR PDBsum; 5ZX3; -.
DR PDBsum; 6BZO; -.
DR PDBsum; 6C04; -.
DR PDBsum; 6C05; -.
DR PDBsum; 6C06; -.
DR PDBsum; 6DV9; -.
DR PDBsum; 6DVB; -.
DR PDBsum; 6DVC; -.
DR PDBsum; 6DVD; -.
DR PDBsum; 6DVE; -.
DR PDBsum; 6EDT; -.
DR PDBsum; 6EE8; -.
DR PDBsum; 6EEC; -.
DR PDBsum; 6FBV; -.
DR PDBsum; 6JCX; -.
DR PDBsum; 6JCY; -.
DR PDBsum; 6KON; -.
DR PDBsum; 6KOO; -.
DR PDBsum; 6KOP; -.
DR PDBsum; 6KOQ; -.
DR PDBsum; 6TYE; -.
DR PDBsum; 6TYF; -.
DR PDBsum; 6TYG; -.
DR PDBsum; 6VVX; -.
DR PDBsum; 6VVY; -.
DR PDBsum; 6VVZ; -.
DR PDBsum; 6VW0; -.
DR PDBsum; 7KIF; -.
DR PDBsum; 7KIM; -.
DR PDBsum; 7KIN; -.
DR AlphaFoldDB; P9WGZ1; -.
DR SASBDB; P9WGZ1; -.
DR SMR; P9WGZ1; -.
DR IntAct; P9WGZ1; 2.
DR STRING; 83332.Rv3457c; -.
DR PaxDb; P9WGZ1; -.
DR DNASU; 887629; -.
DR GeneID; 45427446; -.
DR GeneID; 887629; -.
DR KEGG; mtu:Rv3457c; -.
DR TubercuList; Rv3457c; -.
DR eggNOG; COG0202; Bacteria.
DR OMA; LMKFRNF; -.
DR PhylomeDB; P9WGZ1; -.
DR BRENDA; 2.7.7.6; 3445.
DR Reactome; R-HSA-9639775; Antimicrobial action and antimicrobial resistance in Mtb.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 2.170.120.12; -; 1.
DR Gene3D; 3.30.1360.10; -; 1.
DR HAMAP; MF_00059; RNApol_bact_RpoA; 1.
DR InterPro; IPR011262; DNA-dir_RNA_pol_insert.
DR InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3.
DR InterPro; IPR011773; DNA-dir_RpoA.
DR InterPro; IPR036603; RBP11-like.
DR InterPro; IPR011260; RNAP_asu_C.
DR InterPro; IPR036643; RNApol_insert_sf.
DR PANTHER; PTHR32108; PTHR32108; 1.
DR Pfam; PF01000; RNA_pol_A_bac; 1.
DR Pfam; PF03118; RNA_pol_A_CTD; 1.
DR Pfam; PF01193; RNA_pol_L; 1.
DR SMART; SM00662; RPOLD; 1.
DR SUPFAM; SSF55257; SSF55257; 1.
DR SUPFAM; SSF56553; SSF56553; 1.
DR TIGRFAMs; TIGR02027; rpoA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Nucleotidyltransferase;
KW Reference proteome; Transcription; Transferase.
FT CHAIN 1..347
FT /note="DNA-directed RNA polymerase subunit alpha"
FT /id="PRO_0000175345"
FT REGION 1..226
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT REGION 243..347
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT STRAND 8..15
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 48..58
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:5ZX3"
FT STRAND 93..106
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 133..143
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:7KIF"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:5ZX3"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 204..223
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:6KOQ"
SQ SEQUENCE 347 AA; 37706 MW; E89CA7D377CACF99 CRC64;
MLISQRPTLS EDVLTDNRSQ FVIEPLEPGF GYTLGNSLRR TLLSSIPGAA VTSIRIDGVL
HEFTTVPGVK EDVTEIILNL KSLVVSSEED EPVTMYLRKQ GPGEVTAGDI VPPAGVTVHN
PGMHIATLND KGKLEVELVV ERGRGYVPAV QNRASGAEIG RIPVDSIYSP VLKVTYKVDA
TRVEQRTDFD KLILDVETKN SISPRDALAS AGKTLVELFG LARELNVEAE GIEIGPSPAE
ADHIASFALP IDDLDLTVRS YNCLKREGVH TVGELVARTE SDLLDIRNFG QKSIDEVKIK
LHQLGLSLKD SPPSFDPSEV AGYDVATGTW STEGAYDEQD YAETEQL
