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Database: UniProt
Entry: R5FDU7_9BACT
LinkDB: R5FDU7_9BACT
Original site: R5FDU7_9BACT 
ID   R5FDU7_9BACT            Unreviewed;       332 AA.
AC   R5FDU7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=BN812_01428 {ECO:0000313|EMBL:CCY01804.1};
OS   Prevotella sp. CAG:924.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262938 {ECO:0000313|EMBL:CCY01804.1, ECO:0000313|Proteomes:UP000018357};
RN   [1] {ECO:0000313|EMBL:CCY01804.1, ECO:0000313|Proteomes:UP000018357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:924 {ECO:0000313|Proteomes:UP000018357};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CCY01804.1}.
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DR   EMBL; CAXK010000040; CCY01804.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5FDU7; -.
DR   STRING; 1262938.BN812_01428; -.
DR   Proteomes; UP000018357; 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:UP000018357};
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          21..231
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          255..332
FT                   /note="Alpha C-terminal domain (alpha-CTD)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00059"
SQ   SEQUENCE   332 AA;  37631 MW;  949B0D7EB02F7008 CRC64;
     MAILAFQKPD KVVMLKATDT FGVFEFRPLE PGFGVTIGNA LRRILLSSLE GFAINTIRIS
     GVEHEFSSVP GVKEDVTNII LNLKQVRFKQ VVEEFENEKV SITVENSTEF KAGDIGKYLT
     GFEVLNPELV ICHLDSKASM QIDLTINKGR GYVPADENRQ FCTELNVLPI DSIYTPIRNV
     KYSVEPYRVE QKTDYDKLVI EVTTDGSIHP KDALKEAAKI LIYHFMLFSD GKITLESPDQ
     DDNQKFDFDE EVLHMRQLLK TKLVDMNLSV RALNCLKAAD VETLGDLVQY NKTDLLKFRN
     FGKKSLSELD DLLESLNLSF GTDISKYKLD KE
//
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