ID   RPOB_CAMJE              Reviewed;        1378 AA.
AC   Q46124; Q0PB35; Q9PI31;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 128.
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=Cj0478;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 338-1031.
RX   PubMed=7489896; DOI=10.1016/0378-1119(95)00515-8;
RA   Bustamante V.H., Puente J.L., Sanchez-Lopez F., Bobadilla M., Calva E.;
RT   "Identification of Campylobacter jejuni and C.coli using the rpoB gene and
RT   a cryptic DNA fragment from C.jejuni.";
RL   Gene 165:1-8(1995).
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; AL111168; CAL34626.1; -; Genomic_DNA.
DR   EMBL; X77304; CAA54509.1; -; Genomic_DNA.
DR   PIR; A81393; A81393.
DR   PIR; S41868; S41868.
DR   RefSeq; WP_010891860.1; NC_002163.1.
DR   RefSeq; YP_002343912.1; NC_002163.1.
DR   AlphaFoldDB; Q46124; -.
DR   SMR; Q46124; -.
DR   STRING; 192222.Cj0478; -.
DR   PaxDb; Q46124; -.
DR   PRIDE; Q46124; -.
DR   EnsemblBacteria; CAL34626; CAL34626; Cj0478.
DR   GeneID; 904806; -.
DR   KEGG; cje:Cj0478; -.
DR   PATRIC; fig|192222.6.peg.470; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_3_7; -.
DR   OMA; FMTWEGY; -.
DR   Proteomes; UP000000799; 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; -; 2.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 2.
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; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..1378
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047875"
FT   CONFLICT        338..347
FT                   /note="NDLANGVDAA -> MTWLMALMQP (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        558
FT                   /note="A -> R (in Ref. 2; CAA54509)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        671
FT                   /note="C -> S (in Ref. 2; CAA54509)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        691
FT                   /note="A -> R (in Ref. 2; CAA54509)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1378 AA;  155916 MW;  AB7467C305028EB5 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 SKASLNSDQK IGDKNYKKGQ TADISELEKI
     NRFTLTTLIK AYSKEIQKEY DDLKNHFQNE KKKLKAEHDE KLEILEKDDI LPSGVIKLVK
     VYIATKRKLK VGDKMAGRHG NKGIVSTIVP EVDMPYLPNG KSVDIALNPL GVPSRMNIGQ
     ILESHLGLVG LRLGDQIQEI FDRKQKDFLK ELRAKILEIC SIPRLANEKE FIKSLSDEEL
     LNYARDWSKG VKFSTPVFEG VNIEEFSKLF KMAKIDMDGK TELYDGRTGE KIAERVHVGC
     MYMLKLHHLV DEKVHARSTG PYSLVTQQPV GGKALFGGQR FGEMEVWALE AYGAAHTLRE
     MLTIKSDDVE GRFSAYKALT KGENVPATGI PETFFVLTNE LKSLALDVEI FDKDEDNE