RPOA_LEPIN
ID RPOA_LEPIN Reviewed; 325 AA.
AC Q9XD09;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 129.
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=LA_0765;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Lai / Serogroup Icterohaemorrhagiae / Serovar lai;
RA Zuerner R.L., Harskeer R.A., van de Kemp H., Bal A.E.;
RT "Sequence analysis of a large ribosomal protein gene operon from Leptospira
RT interrogans.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
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}.
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 -!- 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; AF115283; AAD40610.1; -; Genomic_DNA.
DR EMBL; AE010300; AAN47964.1; -; Genomic_DNA.
DR RefSeq; NP_710946.1; NC_004342.2.
DR RefSeq; WP_000054108.1; NC_004342.2.
DR AlphaFoldDB; Q9XD09; -.
DR SMR; Q9XD09; -.
DR STRING; 189518.LA_0765; -.
DR EnsemblBacteria; AAN47964; AAN47964; LA_0765.
DR GeneID; 61142720; -.
DR KEGG; lil:LA_0765; -.
DR PATRIC; fig|189518.3.peg.772; -.
DR HOGENOM; CLU_053084_0_1_12; -.
DR InParanoid; Q9XD09; -.
DR OMA; LMKFRNF; -.
DR Proteomes; UP000001408; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..325
FT /note="DNA-directed RNA polymerase subunit alpha"
FT /id="PRO_0000175327"
FT REGION 1..238
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT REGION 254..325
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT CONFLICT 270
FT /note="V -> A (in Ref. 1; AAD40610)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 325 AA; 36687 MW; AB7DA43FD6CCC2A0 CRC64;
MSLKSLLKGF KRPKKIEFNT EANTPNYGKF VAEPFERGFA TTIGNSLRRT LMSSIEGAAI
SAIRIEGVNH EFSFIEGVAE DVTRIILNLK QVRIKYEPEE KDQSKIIHLE LKGAGYFRAG
DLAVDSSIEI MNPDLHIATL NEDANLVMDL EIQRGRGYVP AEEKKKDIEV LGTIPVDSIF
SPVQKVVFEV SETRVAQRSD YEKLTLEVWT DGSVSPDDAV AQAAKILKEH LTVFINFEEE
LEEEDDELDE ADEKLKASLS KHVEELELSV RSLNVLRSLE IDFIGDLVKR SEEEMSKSKH
YSDQCLQELK VKLSTLGLSF GMRDF
