RPOB_DESVV
ID RPOB_DESVV Reviewed; 1372 AA.
AC A1VAJ6;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Dvul_0439;
OS Desulfovibrio vulgaris subsp. vulgaris (strain DP4).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=391774;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DP4;
RX PubMed=19737303; DOI=10.1111/j.1462-2920.2009.01946.x;
RA Walker C.B., Stolyar S., Chivian D., Pinel N., Gabster J.A., Dehal P.S.,
RA He Z., Yang Z.K., Yen H.C., Zhou J., Wall J.D., Hazen T.C., Arkin A.P.,
RA Stahl D.A.;
RT "Contribution of mobile genetic elements to Desulfovibrio vulgaris genome
RT plasticity.";
RL Environ. Microbiol. 11:2244-2252(2009).
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; CP000527; ABM27462.1; -; Genomic_DNA.
DR RefSeq; WP_011791613.1; NC_008751.1.
DR AlphaFoldDB; A1VAJ6; -.
DR SMR; A1VAJ6; -.
DR PRIDE; A1VAJ6; -.
DR EnsemblBacteria; ABM27462; ABM27462; Dvul_0439.
DR KEGG; dvl:Dvul_0439; -.
DR HOGENOM; CLU_000524_4_0_7; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000009173; 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; 2.40.270.10; -; 2.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR HAMAP; MF_01321; RNApol_bact_RpoB; 1.
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; Transcription;
KW Transferase.
FT CHAIN 1..1372
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300308"
SQ SEQUENCE 1372 AA; 153200 MW; 811040E66AC271C9 CRC64;
MGQLTKKFGK IDVSLPIPHL LNLQVDSYVK FLQEGATERR HDEGLEGVFR SVFPIEDFNR
TASLEFVSYE VGEPKYDQPE CISKGLTYEA PIRIKVRLVV YDVDEDSGNR TIRDIKEQEI
YFGTLPLMTE KGTFIINGTE RVIVNQLQRS PGIIFEHDSG KTHSSRKVLY SCRIIPMRGS
WLDFDFDHKD ILYVRIDRRR KMPATILFKA MGMSKTDILD YFYKKEFYRL DPMGRLMWEV
QKDMYRKDSA FVDIEDGKGG TIVKAGKPIT KRAWRLISEA GLETIEVAPD TIEGMFLAED
IVNPATGEVL AEAADEITAS LVENLREAGI SRLPVLHTKG LETSSSLRDT LVLDKTPDME
AAQVEIYRRL RPSSPPTPEI AASFFDNLFR SADYYDLSPV GRYKLNQRLG IDQSVDLRTL
TDDDILRAIR VLLHLKDSHG PADDIDHLGN RRVRPVGELV ENQYRIGLVR MERAIKERMS
LQEVSTLMPH DLINPKPVAA VLKEFFGTSQ LSQFMDQTNA LSEVTHKRRL SALGPGGLTR
ERAGFEVRDV HTSHYGRICP IETPEGPNIG LIVSLTTYAK VNDFGFIETP YRIIREGALT
DDIKFLDASR EQGEVVAQAN AAVDADGKLA DEYVTARVRG DVLMSHRDEV TLMDISPSQM
VSISAALIPF LEHDDANRAL MGSNMQRQAV PLLRSEKPIV GTGMEGDVAR DSGACILAEG
PGIVRYADAT RIIVSYENGL YPDRGGVRAY DLQKYHKSNQ NSCFGQRPTC HPGQIVKKGD
VLADGPGIED GELALGKNLV VAFMPWCGYN FEDSILISER VVKEDVFTSI HIEEFEVVAR
DTKLGPEEIT RDIPNVGEDM LRNLDGSGII RIGASVKPDD ILVGKITPKG ETQLTPEEKL
LRAIFGDKAR DVKNTSLKVP PGIEGTIIDV KVFNRRSGEK DERTRNIEDY ETARIDKKEQ
DHVRALGDAL RDRLADTLVG KQIAVTLPGK RKGEVLAEAG APMTRELLDA LPVKRLAGLF
KSREVDEMVD TALEDYDRQV AFLKGIYDSK REKVTEGDDL PPGVIKMVKV HIAVKRKLNV
GDKMAGRHGN KGVVSCILPE EDMPFFADGR PVDIVLNPLG VPSRMNIGQI METHLGWGAK
ELGRQLAEML DSGAAMATLR HEVKDVFRSA TIAKLVDEMD DETFRKAVSK LRTGIVTKTP
VFDGASEEDI WSWIERAGMD GDGKTVLYDG RTGDKFYNRV TTGVMYILKL HHLVDEKIHA
RSTGPYSLVT QQPLGGKAQF GGQRLGEMEV WALEAYGASY LLQEFLTVKS DDVTGRVKMY
EKIVKGDNFL EAGLPESFNV LVKELMSLGL NVTLHQEEGK KRPKRVGFMS AL
