RPOB_CAUVN
ID RPOB_CAUVN Reviewed; 1356 AA.
AC B8GZW7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=CCNA_00536;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
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; CP001340; ACL94001.1; -; Genomic_DNA.
DR RefSeq; WP_010918390.1; NC_011916.1.
DR RefSeq; YP_002515909.1; NC_011916.1.
DR AlphaFoldDB; B8GZW7; -.
DR SMR; B8GZW7; -.
DR PRIDE; B8GZW7; -.
DR EnsemblBacteria; ACL94001; ACL94001; CCNA_00536.
DR GeneID; 7332226; -.
DR KEGG; ccs:CCNA_00536; -.
DR PATRIC; fig|565050.3.peg.529; -.
DR HOGENOM; CLU_000524_4_0_5; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR PhylomeDB; B8GZW7; -.
DR Proteomes; UP000001364; 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; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1356
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000165797"
SQ SEQUENCE 1356 AA; 150890 MW; BA113BA0EB7F6B51 CRC64;
MAQSFTGKKR IRKSFGRIPE AVQMPNLIEV QRSSYEQFLQ RETRPGLRRD EGVEAVFKSV
FPIKDFNERA VLEYVSYEFE EPKYDVEECI QRDMTFAAPL KVKLRLIVFE TEEETGARSV
KDIKEQDVYM GDIPLMTDKG TFIVNGTERV IVSQMHRSPG VFFDHDKGKT HASGKLLFAA
RVIPYRGSWL DFEFDAKDIV YVRIDRRRKL PATTFLYALG MDGEEILTTF YDVVPFEKRS
GGWATPYKPE RWRGVKPEFP LVDADTGEEV APAGTKITAR QAKKFADGGL KTLLLAPEAL
TGRYLARDAV NMATGEIYAE AGDELDVTSI QALADQGFST IDVLDIDHVT VGAYMRNTLR
VDKNAIREDA LFDIYRVMRP GEPPTVEAAE AMFKSLFFDA ERYDLSSVGR VKMNMRLEQD
VSDEVRILRK EDVLAVLKVL VGLRDGRGEI DDIDNLGNRR VRSVGELLEN QYRVGLLRME
RAIKERMSSV DIDTVMPHDL INAKPAAAAV REFFGSSQLS QFMDQTNPLS EITHKRRLSA
LGPGGLTRER AGFEVRDVHP THYGRICPIE TPEGPNIGLI NSLATHARVN KYGFIESPYR
RVKDGKPQDE VVYMSAMEES KHVIAQSNIK VAEGEIVEDL VPGRINGEPT LLQKETVDLM
DVSPRQVVSV AAALIPFLEN DDANRALMGS NMQRQAVPLV QSDAPLVGTG MEAVVARDSG
AVVIAKRTGV VEQIDGTRIV IRATEETDPA RSGVDIYRMS KFQRSNQSTC INQRPLVKVG
DRIVAGDIIA DGPSTELGEL ALGRNALVAF MPWNGYNFED SILISERIVR DDVFTSIHIE
EFEVMARDTK LGPEEITRDI PNVGEEALRN LDEAGIVAIG AEVQPGDILV GKVTPKGESP
MTPEEKLLRA IFGEKASDVR DTSLRLPPGV AGTIVDVRVF NRHGVDKDER ALAIERAEID
RLGKDRDDEF AILNRNISGR LKELLIGKVA LSGPKGLSRG EITAEGLAQV ASGLWWQIAL
EDEKAMGELE SLRRLFDENR KRLDRRFEDK VDKLQRGDEL PPGVMKMVKV FVAVKRKLQP
GDKMAGRHGN KGVISRILPI EDMPFLADGT HVDVVLNPLG VPSRMNVGQI FETHLGWACA
NLGKQITNLL EDWQQGGQKQ ALVERLTEIY GPDEELPDTE EGLVELARNL GKGVPIATPV
FDGARMDDIE GHLEMAGVNK SGQSILFDGL TGEQFKRPVT VGYIYMLKLH HLVDDKIHAR
SIGPYSLVTQ QPLGGKAQFG GQRFGEMEVW ALEAYGAAYT LQEMLTVKSD DVAGRTKVYE
SIVRGDDTFE AGIPESFNVL VKEMRSLGLN VELENS
