RPOB_BARBK
ID RPOB_BARBK Reviewed; 1383 AA.
AC A1USC8;
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=BARBAKC583_0571;
OS Bartonella bacilliformis (strain ATCC 35685 / NCTC 12138 / KC583).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=360095;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35685 / NCTC 12138 / KC583;
RA Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S.,
RA Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R.,
RA Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J.,
RA Fraser-Ligget C., Seshadri R.;
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; CP000524; ABM45609.1; -; Genomic_DNA.
DR RefSeq; WP_005766719.1; NC_008783.1.
DR AlphaFoldDB; A1USC8; -.
DR SMR; A1USC8; -.
DR STRING; 360095.BARBAKC583_0571; -.
DR EnsemblBacteria; ABM45609; ABM45609; BARBAKC583_0571.
DR KEGG; bbk:BARBAKC583_0571; -.
DR PATRIC; fig|360095.6.peg.552; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_5; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000000643; 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 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; 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..1383
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300282"
SQ SEQUENCE 1383 AA; 154847 MW; 4B3588930FBD4021 CRC64;
MAQTLAMMSQ FNGRKRVRKF FGKIPEVAEM PNLIEVQKAS YDQFLMIKEP KGGRPDEGLQ
AVFKSVFPIS DFSGTAMLEF VRYEFDAPKF DVEECRQRDL TYAAPLKVIL RLIVFDIDED
TGSKDIKDIK EQGVYMGDMP LMTSNGTFII NGTERVIVSQ MHRSPGVFFD HDKGKSHSSG
KVLFAARVIP YRGSWLDIEF DAKDIVYARI DRRRKIPVTS FLMALGMDAS DILSTFYNKV
TYERVESGWR IPYSVDRFKG VKLVSDLVDA ESGEVVAEAG KKLTARTAKL LVEKGLKAIR
VSEDELLGSY LADDIVNYET GEIYLEAGDE IDEKVLKVLF DVGANQINIL DIDHMSVGAY
IRNTLKVDKN ESRQDALFDI YRVMRPGEPP TIDTAEAMFH SLFFDSERYD LSAVGRVKMN
LRMGLDCPDT VRVLRQEDII GVVKMLVELR DGRGEIDDID NLGNRRVRSV GELMENQYRV
GLLRMERAIK ERMSSVEIDT VMPQDLINAK PAAAAVREFF GSSQLSQFMD QTNPLSEITH
KRRLSALGPG GLTRERAGFE VRDVHPTHYG RICPIETPEG PNIGLINSLA TFARVNKYGF
IESPYRKITD GKVTTEVVYL SAMEEAKHYV AQANSSLDSE GRFTEEFVVC RHAGEVLMVP
RDHIDLMDVS PKQLVSVAAS LIPFLENDDA NRALMGSNMQ RQAVPLIRSE APFVGTGMEA
IVARDSGAAI SAKRGGIVDQ VDATRIVIRA TEDLDPSKSG VDIYRLQKFQ RSNQSTCINQ
RPLVHVGDRI EKGDIIADGP STDLGDLALG RNVLVAFMPW NGYNYEDSIL LSERIVADDV
FTSIHIEEFE VAARDMKLGP EEITRDIPNV AEEALRNLDE AGIVYIGAEV QPGDILVGKI
TPKGESPMTP EEKLLRAIFG EKASDVRDTS MRMPPGTFGT VVEVRVFNRH GVEKDERAME
IEREEIERLA KDRDDEQSIL DRNVYARLAG MLKDKSAIRG PKGFEKGQKI DSTVLNNYPR
SQWWQFAVDD EKVQNKIEAL CNQYDESKEA LQRRFMDKVE KVQRGDEMPP GVMKMVKVFV
AVKRKIQPGD KMAGRHGNKG VVSRILPVED MPFLEDGTHA DIVLNPLGVP SRMNVGQILE
THLGWACAGM GKKIGDLVDF YQETGDILPL RQRIENLIPD NDRNEPVRQY DDESLVKLAH
QMRKGVSIAT PVFDGAHEAD INAMLEDAGL DSSGQVTLYD GRTGEPFDRQ VTVGYIYMLK
LHHLVDDKIH ARSIGPYSLV TQQPLGGKAQ FGGQRFGEME VWALEAYGAA YTLQEMLTVK
SDDVAGRTKV YEAIVRGDDT FEASIPESFN VLIKEMRSLG LNVKLGDARE FMAQQALPEV
VEN
