ID G6E9A8_9SPHN Unreviewed; 352 AA.
AC G6E9A8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=DNA-directed RNA polymerase subunit alpha {ECO:0000256|ARBA:ARBA00015972, ECO:0000256|HAMAP-Rule:MF_00059};
DE Short=RNAP subunit alpha {ECO:0000256|HAMAP-Rule:MF_00059};
DE EC=2.7.7.6 {ECO:0000256|ARBA:ARBA00012418, ECO:0000256|HAMAP-Rule:MF_00059};
DE AltName: Full=RNA polymerase subunit alpha {ECO:0000256|ARBA:ARBA00033070, ECO:0000256|HAMAP-Rule:MF_00059};
DE AltName: Full=Transcriptase subunit alpha {ECO:0000256|ARBA:ARBA00032524, ECO:0000256|HAMAP-Rule:MF_00059};
GN Name=rpoA {ECO:0000256|HAMAP-Rule:MF_00059};
GN ORFNames=NSU_0929 {ECO:0000313|EMBL:EHJ62332.1};
OS Novosphingobium pentaromativorans US6-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1088721 {ECO:0000313|EMBL:EHJ62332.1, ECO:0000313|Proteomes:UP000004030};
RN [1] {ECO:0000313|EMBL:EHJ62332.1, ECO:0000313|Proteomes:UP000004030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=US6-1 {ECO:0000313|EMBL:EHJ62332.1,
RC ECO:0000313|Proteomes:UP000004030};
RX PubMed=22275104; DOI=10.1128/JB.06476-11;
RA Luo Y.R., Kang S.G., Kim S.J., Kim M.R., Li N., Lee J.H., Kwon K.K.;
RT "Genome sequence of benzo(a)pyrene-degrading bacterium Novosphingobium
RT pentaromativorans US6-1.";
RL J. Bacteriol. 194:907-907(2012).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000256|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:0000256|ARBA:ARBA00024550,
CC ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00059}.
CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC {ECO:0000256|ARBA:ARBA00007123, ECO:0000256|HAMAP-Rule:MF_00059}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHJ62332.1}.
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DR EMBL; AGFM01000009; EHJ62332.1; -; Genomic_DNA.
DR RefSeq; WP_007011844.1; NZ_CP009291.1.
DR AlphaFoldDB; G6E9A8; -.
DR STRING; 1088721.JI59_15485; -.
DR KEGG; npn:JI59_15485; -.
DR PATRIC; fig|1088721.3.peg.918; -.
DR eggNOG; COG0202; Bacteria.
DR OrthoDB; 9805706at2; -.
DR Proteomes; UP000004030; Unassembled WGS sequence.
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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd06928; RNAP_alpha_NTD; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 2.170.120.12; DNA-directed RNA polymerase, insert domain; 1.
DR Gene3D; 3.30.1360.10; RNA polymerase, RBP11-like subunit; 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 NCBIfam; TIGR02027; rpoA; 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; SSF47789; C-terminal domain of RNA polymerase alpha subunit; 1.
DR SUPFAM; SSF56553; Insert subdomain of RNA polymerase alpha subunit; 1.
DR SUPFAM; SSF55257; RBP11-like subunits of RNA polymerase; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_00059};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00059}; Reference proteome {ECO:0000313|Proteomes:UP000004030};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00059};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00059}.
FT DOMAIN 28..235
FT /note="DNA-directed RNA polymerase RpoA/D/Rpb3-type"
FT /evidence="ECO:0000259|SMART:SM00662"
FT REGION 1..236
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00059"
FT REGION 262..352
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00059"
SQ SEQUENCE 352 AA; 38449 MW; 7EE70553BDFC3DE3 CRC64;
MTVNIKNWQE LKKPNSLEIK PGPDPKLKAT FVAEPLERGF GLTLGNALRR VLLSSLQGAA
ITSIKIENVL HEFSSLAGVR EDVTDIVLNV KQIALRMQGE GPKRLQLSAT GPAEVKAGDI
AVSGDIEVMN KDLVICHLDE GATLNMELTA DTGKGYVPAV GNRPVDAPIG LIPVDSLYSP
VRQVSYKVEN ARIGQELDFD KLSLTVETDG TVTPEDAVAY SARILQDQLA LFVHFEDIAP
VGAPQMIGMA AAQPEESDTN QLNRYLLKKV DELELSVRSA NCLKNDNIIY IGDLVQKTEA
EMLRTPNFGR KSLNEIKEVL SSMGLRLGMD IPGWPPENIE EMAKKLEQEL LG
//
