RPOB_CAMJ8
ID RPOB_CAMJ8 Reviewed; 1375 AA.
AC A8FKR3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=C8J_0451;
OS Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC
OS 11828).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=407148;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81116 / NCTC 11828;
RX PubMed=17873037; DOI=10.1128/jb.01404-07;
RA Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M.,
RA van Vliet A.H.M.;
RT "The complete genome sequence of Campylobacter jejuni strain 81116
RT (NCTC11828).";
RL J. Bacteriol. 189:8402-8403(2007).
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; CP000814; ABV52050.1; -; Genomic_DNA.
DR AlphaFoldDB; A8FKR3; -.
DR SMR; A8FKR3; -.
DR KEGG; cju:C8J_0451; -.
DR HOGENOM; CLU_000524_4_0_7; -.
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; -; 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; Transcription;
KW Transferase.
FT CHAIN 1..1375
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000329167"
SQ SEQUENCE 1375 AA; 155566 MW; 6525CBC33AC5E0C0 CRC64;
MLDNKLGNRL RVDFSNISKQ IEIPNLLQLQ KKSFDYFLNL DNGESGIEKV FKSIFPIHDP
QNRLSLEYVS SEIGKPKYTI RECMERGLTY SVNLKMKIRL TLHEKDEKTG EKVGVKDIKE
QEIYIREIPL MTDRVSFIIN GVERVVVNQL HRSPGVIFKE EESSTVANKL VYTAQIIPDR
GSWLYFEYDA KDVLYVRINK RRKVPVTMLF RALGYKKQDI IKLFYPIQTI HVKKDKFLTE
FNPNDFMDRI EYDIKDEKGK IVHQAGKRLT KKKAEQLIKD GLKWIEYPVE ILLNRYLANP
IIDKESGEVL FDSLTLLDES KLAKIKEQKS FDIANDLANG VDAAIINSFA QDGETLKLLK
QSENIDDEND LAAIRIYKVM RPGEPVVKDA AKAFVNDLFF NPERYDLTKV GRMKMNHKLG
LEVPEYVTVL TNEDIIKTAK YLIKVKNGKG HIDDRDHLGN RRIRSIGELL ANELHLGLAK
MQKAIRDKFT SLNADLDKVM PYDLINPKMI TTTIIEFFTG GQLSQFMDQT NPLSEVTHKR
RLSALGEGGL VKERAGFEVR DVHATHYGRI CPVETPEGQN IGLINTLSTY AKVNELGFVE
APYRKVVNGK VTNEVVYLTA TQEEGLFIAP ASTKVDAKGN IVEEFVEARQ DGETILARRE
EVQLIDLCSG MVVGVAASLI PFLEHDDANR ALMGSNMQRQ AVPLLTASAP IVGTGMEQII
ARDAWEAVKA KRGGVVEKVD NKSIFILGED DKGPFIDHYT MEKNLRTNQN TNYIQHPIVK
KGDIVKAGQI IADGPSMDQG ELAIGKNALI AFMPWNGYNY EDAIVVSERI IREDTFTSVH
IYEKEIEARE LKDGIEEITK DIPNVKEEDV AHLDESGIAK IGTHIKPGMI LVGKVSPKGE
VKPTPEERLL RAIFGEKAGH VVNKSLYATA SLEGVVVDVK IFTKKGYEKD DRAIKSYDKE
KMALEKEHHD RLLMMDREEM LRVCALLSKA PLNSDQKIGD KNYKKGQTAD ISELEKINRF
TLTTLIKAYS KEIQKEYDDL KNHFQNEKKK LKAEHDEKLE ILEKDDILPS GVIKLVKVYI
ATKRKLKVGD KMAGRHGNKG IVSTIVPEVD MPYLPNGKSV DIALNPLGVP SRMNIGQILE
SHLGLIGLRL GDQIQEIFDR KQKDFLKELR AKMLEICSIP RLASEKEFIK SLSDEELLNY
ARDWSKGVKF ATPVFEGVNI EEFSKLFEMA KIDMDGKTEL YDGRTGEKIA ERVHVGCMYM
LKLHHLVDEK VHARSTGPYS LVTQQPVGGK ALFGGQRFGE MEVWALEAYG AAHTLREMLT
IKSDDVEGRF SAYKALTKGE NVPATGIPET FFVLTNELKS LALDVEIFDK DEDNE
