(data stored in SCRATCH zone)

SWISSPROT: D6XVR8_BACIE

ID   D6XVR8_BACIE            Unreviewed;       314 AA.
AC   D6XVR8;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=DNA-directed RNA polymerase subunit alpha {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|HAMAP-Rule:MF_00059};
DE   AltName: Full=RNA polymerase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00059};
DE   AltName: Full=Transcriptase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00059};
GN   Name=rpoA {ECO:0000256|HAMAP-Rule:MF_00059};
GN   OrderedLocusNames=Bsel_0142 {ECO:0000313|EMBL:ADH97691.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97691.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97691.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC       of DNA into RNA using the four ribonucleoside triphosphates as
CC       substrates. {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:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557,
CC         ChEBI:CHEBI:83400; EC=2.7.7.6; Evidence={ECO:0000256|HAMAP-
CC         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
CC       associated with the core the holoenzyme is formed, which can
CC       initiate transcription. {ECO:0000256|HAMAP-Rule:MF_00059}.
CC   -!- DOMAIN: The N-terminal domain is essential for RNAP assembly and
CC       basal transcription, whereas the C-terminal domain is involved in
CC       interaction with transcriptional regulators and with upstream
CC       promoter elements. {ECO:0000256|HAMAP-Rule:MF_00059}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_00059}.
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DR   EMBL; CP001791; ADH97691.1; -; Genomic_DNA.
DR   RefSeq; WP_013171120.1; NC_014219.1.
DR   STRING; 439292.Bsel_0142; -.
DR   EnsemblBacteria; ADH97691; ADH97691; Bsel_0142.
DR   KEGG; bse:Bsel_0142; -.
DR   eggNOG; ENOG4105CTF; Bacteria.
DR   eggNOG; COG0202; LUCA.
DR   HOGENOM; HOG000218480; -.
DR   KO; K03040; -.
DR   OMA; LMKFRNF; -.
DR   OrthoDB; 662686at2; -.
DR   BioCyc; BSEL439292:G1GLR-167-MONOMER; -.
DR   Proteomes; UP000000271; Chromosome.
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   Pfam; PF01000; RNA_pol_A_bac; 1.
DR   Pfam; PF03118; RNA_pol_A_CTD; 1.
DR   Pfam; PF01193; RNA_pol_L; 1.
DR   ProDom; PD001179; RNAP_asu_C; 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;
DR   PRODOM; D6XVR8.
DR   SWISS-2DPAGE; D6XVR8.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00059,
KW   ECO:0000313|EMBL:ADH97691.1};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00059};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00059};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00059}.
FT   DOMAIN       20    227       RPOLD. {ECO:0000259|SMART:SM00662}.
FT   REGION        1    230       Alpha N-terminal domain (alpha-NTD).
FT                                {ECO:0000256|HAMAP-Rule:MF_00059}.
FT   REGION      247    314       Alpha C-terminal domain (alpha-CTD).
FT                                {ECO:0000256|HAMAP-Rule:MF_00059}.
FT   COILED      231    251       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   314 AA;  35079 MW;  7BD01C3BAED238C8 CRC64;
     MIEIEKPKIE AVELSEDGTY GKFVVEPLER GYGTTLGNSL RRILLNSLPG SAVTSVQFNN
     VLHEFSTIEG VVEDVTTIIL NLKKLSLKIF SEEEKTLEIE AQGEGVITAR DLTHDSDVEV
     LNPDLHIATL SKGAQVQMKV TAKRGRGYVP AEGNNTDDLP IGVIPVDSIF TPVSRVNYQV
     ENTRVGQITN FDKLTLDVWT DGSIRPEEAT SLGAKILNEH LNIFVGLTDQ AQHAEIMVEK
     EEDQKEKVLE MTIEELDLSV RSYNCLKRAG INTVQELTHK SEEDMMKVRN LGRKSLEEVQ
     EKLHELSLGL RKEE
//

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