RPOB_DESAL
ID RPOB_DESAL Reviewed; 1364 AA.
AC B8FEU1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=Dalk_1921;
OS Desulfatibacillum aliphaticivorans.
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfatibacillum.
OX NCBI_TaxID=218208;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK-01;
RX PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT for anaerobic alkane oxidation.";
RL Environ. Microbiol. 14:101-113(2012).
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; CP001322; ACL03618.1; -; Genomic_DNA.
DR RefSeq; WP_012611049.1; NC_011768.1.
DR AlphaFoldDB; B8FEU1; -.
DR SMR; B8FEU1; -.
DR PRIDE; B8FEU1; -.
DR EnsemblBacteria; ACL03618; ACL03618; Dalk_1921.
DR KEGG; dal:Dalk_1921; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_7; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000000739; 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; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
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; 1.
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..1364
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000141684"
SQ SEQUENCE 1364 AA; 152605 MW; 9D5A9A6170DE451A CRC64;
MADRPLTQQR LRKSFGKIAK IVDIPNLIEM QRISYQRFLQ MDVPPEKRET IGLQAVFHSV
FPIRDFSGTA SLEFVSYRFG EIKYSVEDCV HRGMTYEVPI RITVRLVVFD VDKEKGIQNI
RDIKEQEIYF GTIPLMTEQG TFVINGTERV VVSQLHRSSG VFFDHDKGKS HASGKVIYTA
RIIPVRGSWI DMEIDPKDVL YIRIDRRRKF PATLLFKAFG YSTEDLLNYF YQTEKLTLTP
KTLFKEFDAK TLRGQRASIT VKMPDSDEVI VKKGRLFTQR AVKTMAQAGI EKVAILQEDL
EDKVLARRVL DPKTGEVLYP ANHEIDEATL EAMRDAGVQK FEILYSAPGT GGDSVRKALL
LDKVESREEA LVEIYRRLRP SNPSTVEVAK DFIDQLFFRP SHYDLSAVGR MKLNMRLGLD
TPVEVKTLRR EDILLTAKTL VDLKDSQGAV DDIDHLGNRR VRAVGELLEN QYRIGLVRME
RAIKERMSLQ EIDALMPNDL INPKPVSAVV KEFFGTSQLS QFMDQTNPLS EVTHKRRLSA
LGPGGLTRER AGFEVRDVHP SHYGRICPIE TPEGPNIGLI VSLSTYARVN EFGFVETPYR
VVTEGQATKE IKYLSAMEEK DLPIAQANAP LDEEGFFINP TVSSRVEGEL TIVKKEDVKL
MDISPNQLVS VSSSMIPFLE NDDANRALMG SNMQRQAVPL LATEAPLIGT GLERVVARDS
GVTLVAKRDG KVVAVDASRI VLQHEDERKD RMDKQVTIYN LSKFTRSNQN TCFNQRPIVK
LGQEVKAGDI IADGPATENG ELALGRNVTV AFLPWGGYNF EDSILVSERL VRDGVFTSVH
IEEFEVVSRD TKLGKEEITR DIPNVGEEAL KNLDDSGIVR LGAEVRPGDI LVGKITPKGE
TQLSPEEKLL RAIFGEKAGD VKDTSLRVPP GVEGVVVDAK VFARRGVEKD DRTRLIEDEE
IAALEKDRDD ELKIMEDTVR SKLITIVLGQ EATAPVKKGK AVLIPKGQPI TAEMLEDCPL
APLEALVLKD EDHSERVHEL LEIYREQRES VQMSFEEQVN RYQKGDDLPP GVIKMVKIYV
AMKRRLSVGD KMAGRHGNKG VVSCILPQED LPYFENGTPV DMVLNPLGVP SRMNVGQILE
IHLGRAAKSL GDQIEALLEE QKLDGLRQKM QEIFSSDADE VAGLTEQELL EVAGQYKRGV
HMATPVFDGA KEDEITDLLS SAGVSPSGQA VLYDGRTGER FKGEITVGTM YMLKLHHLVD
DKIHARSIGP YSLVTQQPLG GKAQFGGQRL GEMEVWAMEA YGAAYALQEF LTVKSDDMVG
RTRMYEKIVK GQNVLEPGMP ESFNVLVKEL QSLGLEMSLI EEAK