RPOA_MYCS2
ID RPOA_MYCS2 Reviewed; 350 AA.
AC A0QSL8; I7G472;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 101.
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};
GN OrderedLocusNames=MSMEG_1524, MSMEI_1488;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=19926651; DOI=10.1099/mic.0.033670-0;
RA Dey A., Verma A.K., Chatterji D.;
RT "Role of an RNA polymerase interacting protein, MsRbpA, from Mycobacterium
RT smegmatis in phenotypic tolerance to rifampicin.";
RL Microbiology 156:873-883(2010).
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:19926651}.
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:19926651}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000480; ABK71739.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37961.1; -; Genomic_DNA.
DR RefSeq; WP_003892912.1; NZ_SIJM01000016.1.
DR RefSeq; YP_885906.1; NC_008596.1.
DR PDB; 5TW1; X-ray; 2.76 A; A/B/T=1-350.
DR PDB; 5VI5; X-ray; 3.20 A; A/B=1-350.
DR PDB; 5VI8; X-ray; 2.76 A; A/B=1-350, T=251-350.
DR PDB; 6CCE; X-ray; 3.05 A; A/B=1-350.
DR PDB; 6CCV; X-ray; 3.05 A; A/B/T=1-350.
DR PDB; 6DCF; X-ray; 3.45 A; A/B=1-350.
DR PDB; 6EYD; EM; 4.20 A; A/B=1-350.
DR PDB; 6F6W; EM; 3.80 A; A/B=1-350.
DR PDB; 6VVS; X-ray; 3.11 A; A/B/T=1-350.
DR PDB; 6VVT; X-ray; 2.90 A; A/B=1-350.
DR PDB; 6VVV; X-ray; 3.20 A; A/B/T=1-350.
DR PDB; 6YXU; EM; 3.08 A; A/B=1-350.
DR PDB; 6YYS; EM; 3.08 A; A/B=1-350.
DR PDB; 6Z11; EM; 3.36 A; A/B=1-350.
DR PDB; 7P5X; EM; 3.20 A; AA/AB=1-350.
DR PDBsum; 5TW1; -.
DR PDBsum; 5VI5; -.
DR PDBsum; 5VI8; -.
DR PDBsum; 6CCE; -.
DR PDBsum; 6CCV; -.
DR PDBsum; 6DCF; -.
DR PDBsum; 6EYD; -.
DR PDBsum; 6F6W; -.
DR PDBsum; 6VVS; -.
DR PDBsum; 6VVT; -.
DR PDBsum; 6VVV; -.
DR PDBsum; 6YXU; -.
DR PDBsum; 6YYS; -.
DR PDBsum; 6Z11; -.
DR PDBsum; 7P5X; -.
DR AlphaFoldDB; A0QSL8; -.
DR SMR; A0QSL8; -.
DR IntAct; A0QSL8; 2.
DR STRING; 246196.MSMEI_1488; -.
DR PRIDE; A0QSL8; -.
DR EnsemblBacteria; ABK71739; ABK71739; MSMEG_1524.
DR EnsemblBacteria; AFP37961; AFP37961; MSMEI_1488.
DR GeneID; 66732981; -.
DR KEGG; msg:MSMEI_1488; -.
DR KEGG; msm:MSMEG_1524; -.
DR PATRIC; fig|246196.19.peg.1509; -.
DR eggNOG; COG0202; Bacteria.
DR OMA; LMKFRNF; -.
DR OrthoDB; 662686at2; -.
DR BRENDA; 2.7.7.6; 3512.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
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..350
FT /note="DNA-directed RNA polymerase subunit alpha"
FT /id="PRO_0000296835"
FT REGION 1..226
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT REGION 241..350
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT REGION 328..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 14..26
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 31..45
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 48..58
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:6VVT"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:5VI8"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:6YXU"
FT STRAND 93..106
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 133..143
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:5TW1"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:5TW1"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:6VVT"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 171..180
FT /evidence="ECO:0007829|PDB:5TW1"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:6VVT"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 204..218
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:6YYS"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 258..267
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 272..277
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 291..302
FT /evidence="ECO:0007829|PDB:5TW1"
SQ SEQUENCE 350 AA; 37920 MW; 87B23F12DFD648E0 CRC64;
MLISQRPTLS EETVAENRSR FVIEPLEPGF GYTLGNSLRR TLLSSIPGAA VTSIRIDGVL
HEFTTVPGVK EDVTDIILNL KGLVVSSDDD EPVTMYLRKQ GPGVVTAGDI VPPAGVTVHN
PDMHIATLND KGKLEVELVV ERGRGYVPAV QNKASGAEIG RIPVDSIYSP VLKVTYKVEA
TRVEQRTDFD KLIIDVETKN SISPRDALAS AGGTLVELFG LARELNADSE HIEIGPSPAE
ADHIASFALP IDDLDLTVRS YNCLKREGVH TVGELVARTE SDLLDIRNFG QKSIDEVKIK
LHQLGLSLKD SPATFDPSEV AGYDAATGTW TSDAGYDLDD NQDYAETEQL
