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   02-SEP-2026, entry version 89.
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=BT_0895;
OS   Bartonella tribocorum (strain DSM 28219 / CCUG 45778 / CIP 105476 / IBS
OS   506).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Bartonellaceae; Bartonella.
OX   NCBI_TaxID=382640;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28219 / CCUG 45778 / 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=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) +
CC         diphosphate; 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   KEGG; btr:BT_0895; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_3_5; -.
DR   Proteomes; UP000001592; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   CDD; cd00653; RNA_pol_B_RPB2; 1.
DR   FunFam; 2.40.50.100:FF:000006; DNA-directed RNA polymerase subunit beta; 1.
DR   FunFam; 3.90.1800.10:FF:000001; DNA-directed RNA polymerase subunit beta; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1100.10; -; 2.
DR   Gene3D; 2.30.150.10; DNA-directed RNA polymerase, beta subunit, external 1 domain; 1.
DR   Gene3D; 2.40.270.10; DNA-directed RNA polymerase, subunit 2, domain 6; 1.
DR   Gene3D; 3.90.1800.10; RNA polymerase alpha subunit dimerisation domain; 1.
DR   Gene3D; 3.90.1110.10; RNA polymerase Rpb2, domain 2; 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   NCBIfam; NF001616; PRK00405.1; 1.
DR   NCBIfam; TIGR02013; rpoB; 1.
DR   PANTHER; PTHR20856; DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2; 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   SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 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_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
//