RPOB_CAMJJ
ID RPOB_CAMJJ Reviewed; 1378 AA.
AC A1VYJ4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=CJJ81176_0509;
OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=354242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81-176;
RA Fouts D.E., Nelson K.E., Sebastian Y.;
RL Submitted (DEC-2006) 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; CP000538; EAQ73187.2; -; Genomic_DNA.
DR AlphaFoldDB; A1VYJ4; -.
DR SMR; A1VYJ4; -.
DR STRING; 354242.CJJ81176_0509; -.
DR EnsemblBacteria; EAQ73187; EAQ73187; CJJ81176_0509.
DR KEGG; cjj:CJJ81176_0509; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_7; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000000646; 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; 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..1378
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300295"
SQ SEQUENCE 1378 AA; 155944 MW; C48B5A173B9E470F CRC64;
MCDMLDNKLG NRLRVDFSNI SKQIEIPNLL QLQKKSFDYF LNLDNGESGI EKVFKSIFPI
HDPQNRLSLE YVSSEIGKPK YTIRECMERG LTYSVNLKMK IRLTLHEKDE KTGEKVGVKD
IKEQEIYIRE IPLMTDRVSF IINGVERVVV NQLHRSPGVI FKEEESSTVA NKLVYTAQII
PDRGSWLYFE YDAKDVLYVR INKRRKVPVT MLFRALGYKK QDIIKLFYPI QTIHVKKDKF
LTEFNPNDFM DRIEYDIKDE KGKIVHQAGK RLTKKKAEQL IKDGLKWIEY PVEILLNRYL
ANPIIDKESG EVLFDSLTLL DESKLAKIKE QKSFDIANDL ANGVDAAIIN SFAQDGETLK
LLKQSENIDD ENDLAAIRIY KVMRPGEPVV KDAAKAFVND LFFNPERYDL TKVGRMKMNH
KLGLEVPEYV TVLTNEDIIK TAKYLIKVKN GKGHIDDRDH LGNRRIRSIG ELLANELHLG
LAKMQKAIRD KFTSLNADLD KVMPYDLINP KMITTTIIEF FTGGQLSQFM DQTNPLSEVT
HKRRLSALGE GGLVKERAGF EVRDVHATHY GRICPVETPE GQNIGLINTL STYAKVNELG
FVEAPYRKVV NGKVTNEVVY LTATQEEGLF IAPASTKVDA KGNIVEEFVE ARQDGETILA
RREEVQLIDL CSGMVVGVAA SLIPFLEHDD ANRALMGSNM QRQAVPLLTA SAPIVGTGME
QIIARDAWEA VKAKRGGVVE KVDNKSIFIL GEDDKGPFID HYTMEKNLRT NQNTNYIQHP
IVKKGDIVKA GQIIADGPSM DQGELAIGKN ALIAFMPWNG YNYEDAIVVS ERIIREDTFT
SVHIYEKEIE ARELKDGIEE ITKDIPNVKE EDVAHLDESG IAKIGTHIKP GMILVGKVSP
KGEVKPTPEE RLLRAIFGEK AGHVVNKSLY ATASLEGVVV DVKIFTKKGY EKDDRAIKSY
DKEKMALEKE HHDRLLMMDR EEMLRVCALL SKAPLNSDQK IGDKNYKKGQ TADISELEKI
NRFTLTTLIK AYSKEIQKEY DDLKNHFQNE KKKLKAEHDE KLEILEKDDI LPSGVIKLVK
VYIATKRKLK VGDKMAGRHG NKGIVSTIVP EVDMPYLPNG KSVDIALNPL GVPSRMNIGQ
ILESHLGLIG LRLGDQIQEI FDRRQKDFLK ELRAKMLEIC SIPRLASEKE FIKSLSDEEL
LNYARDWSKG VKFATPVFEG VNIEEFSKLF EMAKIDMDGK TELYDGRTGE KIAERVHVGC
MYMLKLHHLV DEKVHARSTG PYSLVTQQPV GGKALFGGQR FGEMEVWALE AYGAAHTLRE
MLTIKSDDVE GRFSAYKALT KGENVPATGI PETFFVLTNE LKSLALDVEI FDKDEDNE