RPOB_XANOM
ID RPOB_XANOM Reviewed; 1383 AA.
AC Q2NZX8;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=XOO3394;
OS Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=342109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 311018;
RA Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT large numbers of effector genes and insertion sequences to its race
RT diversity.";
RL Jpn. Agric. Res. Q. 39:275-287(2005).
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; AP008229; BAE70149.1; -; Genomic_DNA.
DR RefSeq; WP_011260034.1; NC_007705.1.
DR PDB; 6J9F; EM; 3.95 A; C=1-1383.
DR PDBsum; 6J9F; -.
DR AlphaFoldDB; Q2NZX8; -.
DR SMR; Q2NZX8; -.
DR PRIDE; Q2NZX8; -.
DR KEGG; xom:XOO3394; -.
DR HOGENOM; CLU_000524_4_3_6; -.
DR OMA; FMTWEGY; -.
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; 3.
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 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Nucleotidyltransferase;
KW Transcription; Transferase.
FT CHAIN 1..1383
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000237324"
SQ SEQUENCE 1383 AA; 154272 MW; B45F8B13DD1CCFDB CRC64;
MTSYSFTEKK RIRKDFGKQR SILEVPFLLA IQVDSYREFL QEDVESTKRK DLGLHAALKS
VFPISSYSGN AALEYVGYKL GQPVFDEREC RQRGMSYGAP LRVTVRLVIY DRESSTKAIK
YVKEQEVYLG EIPLMTGNGT FIVNGTERVI VSQLHRSPGV FFDHDRGKTH SSGKLLYSAR
IIPYRGSWLD FEFDPKDALF TRIDRRRKLP VSILLRALGY NNEEMLAEFF EINTFHINPD
EGVQLELVPE RLRGETLNFD LADGDKVIVE AGKRITARHV KQLEAAGVAA LAVPDDYLVG
RILSHDVVDG STGELLANAN DEISEDQLTA FRKAGVDAVG TLWVNDLDRG PYLSNTLRID
PTKTQLEALV EIYRMMRPGE PPTKEAAQNL FHNLFFTFER YDLSTVGRMK FNRRVGRKDV
LGESVLYDKK YFAERNDEES KRLVAEHTDT SDILEVIKVL TEIRNGRGVV DDIDHLGNRR
VRSVGEMAEN VFRVGLVRVE RAVKERLSMA ESEGLTPQEL INAKPVAAAI KEFFGSSQLS
QFMDQNNPLS EVTHKRRVSA LGPGGLTRER AGFEVRDVHP THYGRVCTIE TPEGPNIGLI
NSLAVFARTN QYGFLETPYR KVLDGKVSDD VEYLSAIEEN EYVIAQANAL TDAKNMLTEQ
FVPCRFQGES LLKPPSEVHF MDVSPMQTVS VAAALVPFLE HDDANRALMG ANMQRQAVPT
LRSQKPLVGT GIERAVARDS GVTVNALRGG VIEQIDAARI VVKVNEAEIG GGTDAGVDIY
NLIKYTRSNQ NTCINQRPLV NVGDVIARGD VLADGPSTDI GELALGQNML IAFMPWNGYN
FEDSILLSER VVEEDRYTTI HIEELTCVAR DTKLGPEEIS ADIPNVSEQA LNRLDESGVV
YIGAEVRAGD IMVGKVTPKG ESQLTPEEKL LRAIFGEKAS DVKDSSLRVP PGMDGTVIDV
QVFTRDGIEK DKRARQIEEN EIKRVKKDFD DQFRILEAAI YARLRSQIVG KVANGGANLK
KGDSVTDAYL DGLKKSDWFQ LRMKDEDAAD AIERAQKQIQ AHEKEFEARF ADKRGKITQG
DDLAPGVLKM VKVFLAVKRR IQPGDKMAGR HGNKGVVSNV VPVEDMPYMA TGESVDIVLN
PLGVPSRMNI GQILEVHLGW AAKGLGRKIQ RMLEAQAAVS ELRKFLDDIY NHDNAINAQR
VDLSQFSDEE LLNLGKNLID GVPMATPVFD GASEAEIKRM LELADLPQSG QTQLYDGRTG
EAFDRKTTVG YMHYLKLNHL VDDKMHARST GPYSLVTQQP LGGKAQFGGQ RFGEMEVWAL
EAYGAAYTLQ EMLTVKSDDV QGRNQMYKNI VDGEHEMVAG MPESFNVLVK EIRSLAIHME
LEE
