RPOB_BART1
ID RPOB_BART1 Reviewed; 1383 AA.
AC A9ISG1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=BT_0895;
OS Bartonella tribocorum (strain CIP 105476 / IBS 506).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=382640;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 105476 / IBS 506;
RX PubMed=18037886; DOI=10.1038/ng.2007.38;
RA Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G.,
RA Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.;
RT "Genomic analysis of Bartonella identifies type IV secretion systems as
RT host adaptability factors.";
RL Nat. Genet. 39:1469-1476(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; AM260525; CAK01298.1; -; Genomic_DNA.
DR RefSeq; WP_012231479.1; NC_010161.1.
DR AlphaFoldDB; A9ISG1; -.
DR SMR; A9ISG1; -.
DR STRING; 382640.BT_0895; -.
DR PRIDE; A9ISG1; -.
DR EnsemblBacteria; CAK01298; CAK01298; BT_0895.
DR KEGG; btr:BT_0895; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_5; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000001592; 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; Transcription;
KW Transferase.
FT CHAIN 1..1383
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000086361"
SQ SEQUENCE 1383 AA; 155049 MW; 859A248D8C71B5CA CRC64;
MAQTHAMMSQ FNGRKRVRKF FGKIPEVAEM PNLIEVQKAS YDQFLMIEEP KGGRPDEGLQ
AVFKSVFPIS DFSGTAMLEF VGYEFDLPKF DVEECRQRDL TYAAPLKVIL RLIVFDIDED
TGSKDIKDIK EQGVYMGDMP LMTTNGTFIV NGTERVIVSQ MHRSPGVFFD HDKGKSHSSG
KLLFAARVIP YRGSWLDIEF DAKDIIYARI DRRRKIPVTS LLMALGMDGS DILSTFYDKV
TYERDGEGWR VPYSVDRFKG MKLISDLIDA DSGEVVAEAG KKLTVRTAKS LAEKGLKAVK
VSEDDLLGCY LAEDIVNYET GEIYLEAGDE IDEKVLKILL DVRADQINIL DIDHMNIGAY
IRNTLKVDKN ESRQDALFDI YRVMRPGEPP TIDTAEAMFH SLFFDPERYD LSAVGRVKMN
LRMDLDCPDT VRVLRQEDIL AVVKMLVELR DGRGEIDDID NLGNRRVRSV GELMENQYRI
GLLRMERAIK ERMSSVEIDT VMPQDLINAK PAAAAVREFF GSSQLSQFMD QTNPLSEITH
KRRLSALGPG GLTRERAGFE VRDVHPTHYG RICPIETPEG PNIGLINSLA TFARVNKYGF
IESPYRKIID GKVTKEVIYL SAMEEAKHYV AQANSSLDSE GRFTEEFVVC RHAGEVLMAP
RDHVDLMDVS PKQLVSVAAA LIPFLENDDA NRALMGSNMQ RQAVPLVRAE APFVGTGMEA
VVARDSGAAV SAKRSGIVDQ VDATRIVIRA TEDLDPSKSG VDIYRLQKFQ RSNQSTCINQ
RPLVHVGDRV EKGDIIADGP STDLGDLALG RNVLVAFMPW NGYNYEDSIL LSERIVADDV
FTSIHIEEFE VAARDTKLGP EEITRDIPNV AEEALRNLDE AGIIYIGAEV QPGDILVGKI
TPKGESPMTP EEKLLRAIFG EKASDVRDTS MRMPPGTFGT VVEVRVFNRH GVEKDERAMA
IEREEIERLA KDRDDEQSIL DRNVYARLTD MLTGKVAVEG PKGFSESKKL DSTVMGRYPR
SQWWQFAVED EKLQNEIEAL RKQYDESKEA LQRRFMDKVE KVQRGDEMPP GVMKMVKVFV
AVKRKIQPGD KMAGRHGNKG VVSRILPVED MPFLEDGTHA DIVLNPLGVP SRMNVGQILE
THLGWACAGM GKKIGDLLEL YQETGDILPL RQRIENLMPD DNHNEPVRQY DNESLYKLAL
QMKKGVSIAT PVFDGAHESD INMMLEDAGL DSSGQVTLYD GRTGEPFDRP VTVGYIYMLK
LHHLVDDKIH ARSIGPYSLV TQQPLGGKAQ FGGQRFGEME VWALEAYGAA YTLQEMLTVK
SDDVAGRTKV YEAIVRGDDT FEAGIPESFN VLVKEMRSLA LNVELDDARE LIAQRVLSDR
VEQ
