RPOB_MARSD
ID RPOB_MARSD Reviewed; 1366 AA.
AC C6C179;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE Short=RNAP subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; OrderedLocusNames=Desal_1179;
OS Maridesulfovibrio salexigens (strain ATCC 14822 / DSM 2638 / NCIMB 8403 /
OS VKM B-1763) (Desulfovibrio salexigens).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Maridesulfovibrio.
OX NCBI_TaxID=526222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14822 / DSM 2638 / NCIMB 8403 / VKM B-1763;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA Wall J.D., Arkin A.P., Dehal P., Chivian D., Giles B., Hazen T.C.;
RT "Complete sequence of Desulfovibrio salexigens DSM 2638.";
RL Submitted (JUN-2009) 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:0000255|HAMAP-Rule:MF_01321}.
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:0000255|HAMAP-Rule:MF_01321};
CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC and 1 omega subunit. When a sigma factor is associated with the core
CC the holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR EMBL; CP001649; ACS79242.1; -; Genomic_DNA.
DR RefSeq; WP_015851061.1; NC_012881.1.
DR AlphaFoldDB; C6C179; -.
DR SMR; C6C179; -.
DR STRING; 526222.Desal_1179; -.
DR EnsemblBacteria; ACS79242; ACS79242; Desal_1179.
DR KEGG; dsa:Desal_1179; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_7; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000002601; Chromosome.
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:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.30.150.10; -; 1.
DR Gene3D; 2.40.270.10; -; 2.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 2.
DR HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR InterPro; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf.
DR InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR010243; RNA_pol_bsu_bac.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 2.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF10385; RNA_pol_Rpb2_45; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR TIGRFAMs; TIGR02013; rpoB; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1366
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000214473"
SQ SEQUENCE 1366 AA; 153015 MW; C1B778F718713BA4 CRC64;
MGQLRKIFGK IKVTLPIPHL LELQVDSFKK FLQEGVAPAS RADVGLEGVF RSVFPIEDFN
KTASLEYVSY DIGEPKYDMD ECISKGLTYE APIRIKVRLV VFDVDEETES RTIRDIKEQD
IYFGTVPLMS EQGTFIINGT ERVIVNQLQR SPGIIFEHDS GKTHTSRKVL YSCRIIPMRG
SWLDFDFDHK DILYVRIDRR RKMPATVLLK AMGLSKQDIL DYYYDVEEYQ IDRHIVRRKV
VENQYRKENA WVDLCLEDGK VIVARDKQIT KFGWKKLVRG GVEYIEVDPK SLVGQFAFND
ITDPDTGEVI AEAADEITEE IFERIQEVGL KDVKVLHTQG ADVSSALRDS MMLDKTTDVE
SAQIEIYRRL RPSSPPTAEI AANFFENLFR SSDYYDLSSV GRYKLNARLN IETPLELRTL
TNEDILTAVK VLCKLKDSHG PADDIDNLGN RRVRPVGELV ENQYRIGLVR MERAIKERMS
LQEVATLMPH DLINPKPVAA VLKEFFGTSQ LSQFMDQTNP LSEVTHKRRL SALGPGGLTR
ERAGFEVRDV HVSHYGRICP IETPEGPNIG LIVSLTTYSK VNDFGFIESP YRTIKDSTMT
DEILYYDATR EVGHVVAQAN APIDEKGSFT NPLVTCRLNG DVSMHPREDA TLMDISPSQT
VSVSAALIPF LEHDDANRAL MGSNMQRQAV PLLKTSQPLV GTGMEANVAQ DSGSCVLAEN
DGVIDYVDAE RLVVRYDDGV YPDTGGVKHY ELQKWHKSNQ NSCYGQRPRL PIGTPVKKGD
VLADGPGIKD GELALGKNLL VAFMPWCGYN FEDSILISER VVKEDVFTSV HIEEFELVAR
DTKLGPEEVT RDIPNVSEEM LRNLDECGII RLGARIAPDD ILVGKITPKG ETQLTPEEKL
LRAIFGDKAR DVKNTSLKVP PGIEGTVVDV KVFNRRSGEK DDRTRNIEDF ELAKHDMKES
KHIESLTNKT RVKIADVVAN KQIAQTLMGR KKGEVLAEAG HIITDEILAE VPLKKLGGLF
ADKETNEAVK QLLAEYDKQI RIIKGIYDVK REKVTEGDDL PPGVIKMVKV YIAVKRKLSV
GDKMAGRHGN KGVVSNILPE QDMPFFDNGT PMDIVLNPLG VPSRMNIGQI METHLGWAAL
ALGQKFAAML DTGEALGVIR QEIKDTFESE DVYELIDSLD DEEFRLAVNK AREGIVTKTP
VFDGATEEEI WDLVGKTGIG DDGKVTLYDG RTGDPFHNRV TVGVMYILKL HHLVDEKIHA
RSTGPYSLVT QQPLGGKAQF GGQRLGEMEV WALEAYGAAY LLQEFLTVKS DDVTGRVKMY
EKIVKGDNFL EAGLPESFNV LVKELMSLGL DVNLLQDEVE ETADKK