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ID D6XVN3_BACIE Unreviewed; 1201 AA.
AC D6XVN3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 08-MAY-2019, entry version 66.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE Short=RNAP subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01322};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
GN Name=rpoC {ECO:0000256|HAMAP-Rule:MF_01322};
GN OrderedLocusNames=Bsel_0107 {ECO:0000313|EMBL:ADH97656.1};
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:ADH97656.1, ECO:0000313|Proteomes:UP000000271};
RN [1] {ECO:0000313|EMBL:ADH97656.1, 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_01322,
CC ECO:0000256|RuleBase:RU004279, ECO:0000256|SAAS:SAAS00054030}.
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_01322, ECO:0000256|RuleBase:RU004279,
CC ECO:0000256|SAAS:SAAS01121830};
CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1
CC beta' and 1 omega subunit. When a sigma factor is associated with
CC the core the holoenzyme is formed, which can initiate
CC transcription. {ECO:0000256|HAMAP-Rule:MF_01322}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|HAMAP-Rule:MF_01322, ECO:0000256|RuleBase:RU004279}.
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DR EMBL; CP001791; ADH97656.1; -; Genomic_DNA.
DR RefSeq; WP_013171086.1; NC_014219.1.
DR STRING; 439292.Bsel_0107; -.
DR EnsemblBacteria; ADH97656; ADH97656; Bsel_0107.
DR KEGG; bse:Bsel_0107; -.
DR eggNOG; ENOG4105D27; Bacteria.
DR eggNOG; COG0086; LUCA.
DR HOGENOM; HOG000218387; -.
DR KO; K03046; -.
DR OMA; QGVEIND; -.
DR OrthoDB; 4421at2; -.
DR BioCyc; BSEL439292:G1GLR-131-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:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR InterPro; IPR012754; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 2.
DR SMART; SM00663; RPOLA_N; 1.
DR TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
PE 3: Inferred from homology;
DR PRODOM; D6XVN3.
DR SWISS-2DPAGE; D6XVN3.
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_01322,
KW ECO:0000256|RuleBase:RU004279, ECO:0000256|SAAS:SAAS00442970,
KW ECO:0000313|EMBL:ADH97656.1};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01322,
KW ECO:0000256|RuleBase:RU004279, ECO:0000256|SAAS:SAAS00442967};
KW Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW Transcription {ECO:0000256|HAMAP-Rule:MF_01322,
KW ECO:0000256|RuleBase:RU004279, ECO:0000256|SAAS:SAAS00442998};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01322,
KW ECO:0000256|RuleBase:RU004279, ECO:0000256|SAAS:SAAS00443006}.
FT DOMAIN 224 503 RPOLA_N. {ECO:0000259|SMART:SM00663}.
FT COILED 666 686 {ECO:0000256|SAM:Coils}.
SQ SEQUENCE 1201 AA; 134426 MW; 6B9BD35A3B9C1797 CRC64;
MIDVNNFEYM KIGLASSDKI RSWSRGEVKK PETINYRTLK PEKDGLFCER IFGPTKDWEC
HCGKYKRVRY KGVVCDRCGV EVTRAKVRRE RMGHIELAAP VSHIWYFKGI PSRMGLVLDM
SPRSLEEVIY FASYVVTDPG ETPLETKQLL SEKEYRAYYD KYGRSFKATM GAEAIRKLLE
DIDLDKEADM LKEELETAQG QRRTRAIKRL EVLEAFRHSD NDPSWMVLDV LPVIPPELRP
MVQLDGGRFA TSDLNDLYRR VINRNNRLKR LLDLGAPSII VQNEKRMLQE AVDALIDNGR
RGRPVTGPGN RPLKSLSHML KGKQGRFRQN LLGKRVDYSG RSVIVVGPNL KMYQCGLPKE
MALELFKPFV MKELVGQGLA HNIKSAKRKV ERVQPEVWDV LEDIIKEHPV LLNRAPTLHR
LGIQAFEPIL VEGRAIKLHP LVCTAYNADF DGDQMAVHVP LSAEAQAESR LLMLAAQNIL
NPKDGKPVVT PSQDMVLGNY YLTLERENAV GEGSIFTGPN EVLSAYQAGY VHLHTRIAMP
VTSINKTNFE DAVQDHYLLT SVGKVIFNEI LPDSFPYINE PSAVNLEEVT PRKYFVPRGT
DIKAEFKERE LISPFKKGFL GDIIAEVFKK FKISETSVML DKMKELGFYY STKAGITIGV
SDIVVLKDKQ DILDEADEKV TRVTKQFRRG LITEEERYDK VIEIWSNAKD VIQEKLLGTL
VKTNPIFMMS DSGARGNASN FTQLAGMRGL MANPSGRIIE LPIKSSFREG LTVLEYFIST
HGARKGLADT ALKTADSGYL TRRLVDVAQD VIIRTDDCGT DRGLEVKAIK EGTEVIESLY
DRLVGRVSFQ RIYHPETGEL LADRNQDITE DMAKVIEDAG VQNVMIRSVF TCDTKHGACK
KCYGRNLATG AEVEVGEAVG IIAAQSIGEP GTQLTMRTFH TGGVAGDDIT QGLPRIQEVF
EARNPKGQAV ISEIEGTVAE IKDQNDKKEI VIQGPVETRN YPTMYGARMK VKEGDTILAG
QELTEGSIDP KELLQVSGVQ GVQEYLLREV QKVYRMQGVE IGDKHVEVMV RQMMRKVRVI
DSGDTDILPG SLVEIHQYSD ANREVLLKGG RPATGRPVLL GITKASLETD SFLSAASFQE
TTRVLTDAAI KGKRDQLVGL KENVIIGKLV PAGTGMQRYR QLKAVNTEDN SDIIEQPAGT
E
//
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