ID M7P706_9BACL Unreviewed; 313 AA.
AC M7P706;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
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 ECO:0000313|EMBL:EMR06299.1};
GN ORFNames=C772_01570 {ECO:0000313|EMBL:EMR06299.1};
OS Bhargavaea cecembensis DSE10.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Bhargavaea.
OX NCBI_TaxID=1235279 {ECO:0000313|EMBL:EMR06299.1, ECO:0000313|Proteomes:UP000011919};
RN [1] {ECO:0000313|EMBL:EMR06299.1, ECO:0000313|Proteomes:UP000011919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE10 {ECO:0000313|EMBL:EMR06299.1,
RC ECO:0000313|Proteomes:UP000011919};
RX PubMed=23766406;
RA Shivaji S., Ara S., Begum Z., Ruth M., Singh A., Kumar Pinnaka A.;
RT "Draft Genome Sequence of Bhargavaea cecembensis Strain DSE10T, Isolated
RT from a Deep-Sea Sediment Sample Collected at a Depth of 5,904 m from the
RT Chagos-Laccadive Ridge System in the Indian Ocean.";
RL Genome Announc. 1:e00346-13(2013).
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:EMR06299.1}.
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DR EMBL; AOFT01000007; EMR06299.1; -; Genomic_DNA.
DR RefSeq; WP_008298847.1; NZ_AOFT01000007.1.
DR AlphaFoldDB; M7P706; -.
DR STRING; 1235279.C772_01570; -.
DR PATRIC; fig|1235279.3.peg.1567; -.
DR eggNOG; COG0202; Bacteria.
DR OrthoDB; 9805706at2; -.
DR Proteomes; UP000011919; 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:UP000011919};
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 19..226
FT /note="DNA-directed RNA polymerase RpoA/D/Rpb3-type"
FT /evidence="ECO:0000259|SMART:SM00662"
FT REGION 1..229
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00059"
FT REGION 246..313
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00059"
SQ SEQUENCE 313 AA; 34876 MW; 7E8B3256E7C4676C CRC64;
MIEIEKPRIE AVQTVENTYG KFIVEPLERG YGTTLGNSLR RILLSSLPGA AVTSIQIDGV
LHEFSTVDGV VEDVASIILN VKQLALKIYS DDEKVIEIDV KGESEVTAAD ITHDSDVEIL
NPDLHIATVG KNGHLRMRMY AQRGRGYVPA DRNKREDLPI GVIPIDSIYT PVSRVNFQVE
NTRVGQLSDY DKLTLDVWTD GSIGPQEAIS LGSRILTEHL NIFVGLTDEA QSVEIMVEKE
EDQKEKVLEM TIEELDLSVR SYNCLKRAGI NTVLELANKT EDEMMKVRNL GRKSLEEVKA
KLTDLGLGLR TEE
//
