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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
 
 
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