RPOB_XYLFM
ID RPOB_XYLFM Reviewed; 1384 AA.
AC B0U5X7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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};
GN OrderedLocusNames=Xfasm12_2196;
OS Xylella fastidiosa (strain M12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=405440;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M12;
RX PubMed=20601474; DOI=10.1128/jb.00651-10;
RA Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT causing almond leaf scorch disease in California.";
RL J. Bacteriol. 192:4534-4534(2010).
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; CP000941; ACA13049.1; -; Genomic_DNA.
DR RefSeq; WP_004084689.1; NC_010513.1.
DR AlphaFoldDB; B0U5X7; -.
DR SMR; B0U5X7; -.
DR PRIDE; B0U5X7; -.
DR KEGG; xfm:Xfasm12_2196; -.
DR HOGENOM; CLU_000524_4_0_6; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
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; -; 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; 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..1384
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000141753"
SQ SEQUENCE 1384 AA; 154296 MW; D57B78ACEBADBD16 CRC64;
MTSYSFTEKK RIRKDFGKHR SILKVPFLLA IQVDSYRAFL QGDVESSQRK DIGLHGALKS
VFPIVSYSGN AALEYVGYKL GEPMFDEREC RQRGMSYGAP LRVTVRLVIY DRESSTKAVK
YIKEQEVYLG EIPLMTENGT FIVNGTERVI VSQLHRSPGV FFDHDRGKTH SSGKLLYSAR
IIPCRGSWLD FEFDPKDALF TRIDRRRKLP VSILLRALGY SNEEILGEFF EINTFHINPD
KGVQLELVPE RLRGEILSFN LTDGGGVIVE AGKRITARHV KQLEASGISA LAVPDDYLIG
RILSHDVIDA TTGELLASAN SEVNEDRIVA FRKAGIESVG TLWVNDLDRG AYLSNTLRID
PTRTQLEAQV EIYRMMRPGE PPTKEAAQNL FHNLFFTFDR YDLSMVGRMK FNRRVGRKEV
AGEPVLYDKK YFSDRNDEES RRLVSKLGET SDILDVIKGL CEIRNGRGVV DDIDHLGNRR
VRSVGEMAEN VFRVGLVRVE RAVKERLSMA ESEGLTPQEL INAKPVAAAI KEFFGSSQLS
QFMDQNNPLS EVTHKRRLSA LGPGGLTRER AGFEVRDVHL SHYGCLCTIE TPEGPNIGLI
NSLAVFARTN QYGFLETPYR KVVEGRVTDE VEYLSAIEEN QYVIAQANTL TDDNGQLTES
FVPCRFQGES LLKPPSYVHY MDVSPMQTVS VAAALVPFLE HDDANRALMG ANMQRQAVPT
LRAQKPLVGT GIERTVALDS GVTVNARRGG VIDQVDAGRI VVKVNESEII GATDAGVDIY
GLIKYTRSNQ NTCINQRPLV NVGDIIASGD VLADGPSTDI GELALGQNML IAFMPWNGYN
FEDSILLSER VVEEDRYTTI HIEELTCIAR DTKLGSEEIS ADIPNVSEQA LNRLDESGVV
YIGAEVRAGD ILVGKVTPKG ESQLTPEEKL LRAIFGEKAS DVKDSSLRVP PGMDGTVIDV
QVFTRDGIEK DKRAHQIEEY EIKRVKKDFD DQFRILEGAI YARLRSQIVG KVVNSGVDIK
KGEVITGPYL DGLKKSDWFA LRMKDEVAVE AIDRAQKQIQ AYQKEFDQRF SDKRSKITQG
DDLAPGVLKM VKVFLAVKRC IQCGDKMAGR HGNKGVISNI VPVEDMPFME DGTPVDIVLN
PLGVPSRMNI GQILEVHLGW AAKGLGHRIQ RMLEANAAIA DLRKFLNEIY NHDKSLVGER
VDLSQFSDDE LLNMAKNLTD GVPMASPVFD GASEQEIKRM LDLAELPTGG QTQLYDGHTG
EPFDRKTTVG YMHYLKLNHL VDDKMHARST GPYSLVTQQP LGGKAQFGGQ RFGEMEVWAL
EAYGAAYTLQ EMLTVKSDDV QGRNQMYKNI VDGDHQMVAG MPESFNVLVK EIRSLAINIE
LEDN
