ID   RPOB_BARHE              Reviewed;        1383 AA.
AC   Q9KJG4;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=BH06100;
OS   Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS   (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX   PubMed=11158086; DOI=10.1128/jcm.39.2.430-437.2001;
RA   Renesto P., Gouvernet J., Drancourt M., Roux V., Raoult D.;
RT   "Use of rpoB gene analysis for detection and identification of Bartonella
RT   species.";
RL   J. Clin. Microbiol. 39:430-437(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT   of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; AF171070; AAF87049.1; -; Genomic_DNA.
DR   EMBL; BX897699; CAF27414.1; -; Genomic_DNA.
DR   RefSeq; WP_011180534.1; NZ_LRIJ02000001.1.
DR   AlphaFoldDB; Q9KJG4; -.
DR   SMR; Q9KJG4; -.
DR   STRING; 283166.BH06100; -.
DR   PaxDb; Q9KJG4; -.
DR   PRIDE; Q9KJG4; -.
DR   EnsemblBacteria; CAF27414; CAF27414; BH06100.
DR   GeneID; 64156889; -.
DR   KEGG; bhe:BH06100; -.
DR   eggNOG; COG0085; Bacteria.
DR   OMA; FMTWEGY; -.
DR   Proteomes; UP000000421; 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..1383
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047862"
SQ   SEQUENCE   1383 AA;  154853 MW;  2CEE87E06A3207B6 CRC64;
     MAQTLAMTSQ FNGRKRVRKF FGKIPEVAEM PNLIEVQKAS YDQFLMIEEP KGGRPDEGLQ
     AVFKSVFPIS DFSGTAMLEF VGYQFDSPKF DVEECRQRDL TYAAPLKVIL RLIVFDVDED
     TGSKDIKDIK EQGVYMGDMP LMTTNGTFIV NGTERVIVSQ MHRSPGVFFD HDKGKSHSSG
     KFLFAARVIP YRGSWLDIEF DAKDIIYARI DRRRKIPVTS LLMALGMDAS DILSTFYNKV
     TYERDGDGWR IPYSVDRFKG MKLVSDLIDA DSGEVVAEAG KKLTVRAAKA LAEKGLKAVK
     VSEDDLLGSY LAEDIVNYQT GEIYLEAGDE IDEKTLRVLF DVNADQIDIL DIDHMNIGAY
     IRNTLKVDKN ESRQDALFDI YRVMRPGEPP TMDTAEAMFH SLFFDPERYD LSAVGRVKMN
     LRMDLDCPDT VRVLRQEDIL AVVKMLVELR DGRGEIDDID NLGNRRVRSV GELMENQYRI
     GLLRMERAIK ERMSSVEIDT VMPQDLINAK PAAAAVREFF GSSQLSQFMD QTNPLSEITH
     KRRLSALGPG GLTRERAGFE VRDVHPTHYG RICPIETPEG PNIGLINSLA TFARVNKYGF
     IESPYRKIID GKVTTEVIYL SAMEESKHYV AQANSSLDAE GRLSEEFVVC RHAGEVLMAP
     RDHVDLMDVS PKQLVSVAAA LIPFLENDDA NRALMGSNMQ RQAVPLVRAE APFVGTGMES
     IVARDSGAAV AARRSGIVDQ VDATRIVIRA TEDLDPSKSG VDIYRLQKFQ RSNQSTCINQ
     RPLVHVGDRV EKGNIIADGP STDLGDLALG RNVLVAFMPW NGYNYEDSIL LSERIVADDV
     FTSIHIEEFE VAARDTKLGP EEITRDIPNV AEEALRNLDE AGIIYIGAEV QPGDILVGKI
     TPKGESPMTP EEKLLRAIFG EKASDVRDTS MRMPPGAFGT VVEVRVFNRH GVEKDERAMA
     IEREEIERLA KDRDDEQSIL DRNVYARLTD MLVGKVAVEG PKGFSKNKKL DTTIMGHYPR
     SQWWQFTVED EKLQNEIEAL RNQYDESKEA LQRRFMDKVE KVQRGDEMPP GVMKMVKVFV
     AVKRKIQPGD KMAGRHGNKG VVSRILPIED MPFLEDGTHA DIVLNPLGVP SRMNVGQILE
     THLGWACAGM GKKIGDLVDL YQETGDILPL RQRIENLMPD DDHNEPVRQY DNESLYKLAL
     QMRKGVSIAT PVFDGAHEAD INMMLEDAGL DSSGQVTLYD GRTGEPFDRP VTVGYIYMLK
     LHHLVDDKIH ARSIGPYSLV TQQPLGGKAQ FGGQRFGEME VWALEAYGAA YTLQEMLTVK
     SDDVAGRTKV YEAIVRGDDT FEAGIPESFN VLVKEMRSLA LNVELDDARE LIAQRALSDT
     TEQ