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RPOB_CAMLR
ID   RPOB_CAMLR              Reviewed;        1377 AA.
AC   B9KFG7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Cla_0449;
OS   Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=306263;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM2100 / D67 / ATCC BAA-1060;
RX   PubMed=18713059; DOI=10.1089/fpd.2008.0101;
RA   Miller W.G., Wang G., Binnewies T.T., Parker C.T.;
RT   "The complete genome sequence and analysis of the human pathogen
RT   Campylobacter lari.";
RL   Foodborne Pathog. Dis. 5:371-386(2008).
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; CP000932; ACM63802.1; -; Genomic_DNA.
DR   RefSeq; WP_012661185.1; NC_012039.1.
DR   AlphaFoldDB; B9KFG7; -.
DR   SMR; B9KFG7; -.
DR   STRING; 306263.Cla_0449; -.
DR   PRIDE; B9KFG7; -.
DR   EnsemblBacteria; ACM63802; ACM63802; CLA_0449.
DR   GeneID; 7411186; -.
DR   KEGG; cla:CLA_0449; -.
DR   PATRIC; fig|306263.5.peg.446; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_0_7; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000007727; 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; Transcription;
KW   Transferase.
FT   CHAIN           1..1377
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_1000165796"
SQ   SEQUENCE   1377 AA;  155941 MW;  8A5C8A186BBAA378 CRC64;
     MLNSQSGNRL RIDFSNVPQQ IDIPNLLQLQ KKSFDYFLNI DAKNSESGIE KVFKSIFPIH
     DPQNRLSLEY VSSEVGKPKY TIRECMERGL TYSVNLKMKI RLTLHEKDEK TGEKIGIKDI
     KEQEIYIREI PLMTDRISFI INGVERVVVN QLHRSPGVIF KEEESSTVAN KLVYTAQIIP
     DRGSWLYFEY DAKDVLYVRI NKRRKVPITI LFRALGYKKQ DIIKLFYPIQ TIHVKKDKFL
     TEFNPNDFLD RVEYDLKDEK GNIIHQAGKR MTKKKAEQLV KDGIKWVEYP VEILTNRYLA
     NPIINKETGE VLFDSLTLLD ESKLAKIKEQ KTFDIANDLA NGVDAAIINS FIQDNETLKL
     LKQTENIDDE NDLAAIRIYK VMRPGEPVVK DAAKAFVNDL FFNPERYDLT KVGRMKMNHK
     LGLDTPEYVT VLTNEDIVKT AKYLIKVKNG RGHIDDRDHL GNRRIRSIGE LLANELHVGL
     AKMQKAIRDK FTALNTDIDK VMPYDLINPK TITVTIMEFF TGGQLSQFMD QTNPLSEVTH
     KRRLSALGEG GLVKERAGFE VRDVHATHYG RICPVETPEG QNIGLINTLS TYAKVNDLGF
     VEAPYKKVEN GKVSNEIVYL TATQEEGLVI AAASTKIDEK GSIVEEFVEA RQDGETILAR
     REEVHLIDLC SGMIVGVAAS LIPFLEHDDA NRALMGSNMQ RQAVPLLTAQ APIVGTGMEK
     IIARDAWEAI KAKRAGIVEK VDNKNIFILG EDENGPFIDH YKMEKNLRTN QNTTFTQHPI
     VKKGEFVQVG QIIADGPSMD QGELAIGKNA LIAFMPWHGY NYEDAIVISE KILREDTFTS
     VHIYEKEVEA RELKDGVEEI TKDIPNVKED DLAHLDESGI AKIGTHIKPG MILVGKVSPK
     GEVKPTPEER LLRAIFGEKA GHVVNKSLYA TASMEGVVVD VKIFTKKGYE KDARAIKAYD
     EEKLNLEKEH HDRLLMMDRE ETLRVCSLLS KSALNSDEEI NGQKYKKGAK VDIKELEKIN
     RFALNSLVKA YSKDVQKEYE DLKNHFQNEK KKLKSEHDEK LEILEKDDIL PSGVVKLVKV
     YIATKRKLKV GDKMAGRHGN KGIVSNIVPE VDMPYLPDGR PIDIALNPLG VPSRMNIGQI
     LESHLGIVGM RLGDQIQEIF DKKQKDFIKQ LRTKILEICS VSRLTLEKKF VESLNDEQLI
     SYARDWARGV KFATPVFEGV TVEEFSKLFE MAKIAMDGKS ELYDGRTGEK MAERVHVGCM
     YMLKLHHLVD EKVHARSTGP YSLVTQQPVG GKALFGGQRF GEMEVWALEA YGAAHTLREM
     LTIKSDDVEG RFSAYKALTK GENVPATGIP ETFFVLTNEL KSLALDVEIF DKDENNE
 
 
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