ID   RPOB_BARQU              Reviewed;        1383 AA.
AC   Q9KJM5; Q6FZL9;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   03-AUG-2022, entry version 112.
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=BQ07130;
OS   Bartonella quintana (strain Toulouse) (Rochalimaea quintana).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC VR-358 / Fuller / CIP 107027;
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=Toulouse;
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; AF165994; AAF80850.1; -; Genomic_DNA.
DR   EMBL; BX897700; CAF26202.1; -; Genomic_DNA.
DR   RefSeq; WP_011179456.1; NC_005955.1.
DR   AlphaFoldDB; Q9KJM5; -.
DR   SMR; Q9KJM5; -.
DR   STRING; 283165.BQ07130; -.
DR   EnsemblBacteria; CAF26202; CAF26202; BQ07130.
DR   KEGG; bqu:BQ07130; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_3_5; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000000597; 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_0000047863"
FT   CONFLICT        191
FT                   /note="Y -> N (in Ref. 1; AAF80850)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1383 AA;  154830 MW;  B559BB6E0BF4BE6A CRC64;
     MAQTLAMTSQ FNGRKRVRKF FGKIPEVTEM PNLIEVQKAS YDQFLMIEEP KGGRPDEGLQ
     AVFKSVFPIS DFSGTAMLEF VGYEFDLPKF DVEECRQRDL TYAAPLKVIL RLIVFDVDED
     TGSKDIKDIK EQGVYMGDMP LMTTNGTFIV NGTERVIVSQ MHRSPGVFFD HDKGKSHSSG
     KFLFAARVIP YRGSWLDIEF DAKDIIYARI DRRRKIPITS LLMALGMDAS DILSTFYNKV
     TYERDGDGWR IPYSVGRFKG VKLISDLVDA DSGEVVAEAG KKLTVRAAKA LAEKGLKAVK
     ITEDDLLGSY LAEDIVNYQT GEIYLEAGDE IDEKALKILF DVSADQINIL DIDHMNIGAY
     IRNTLKVDKN ESQQDALFDI YRVMRPGEPP TMDTAAAMFH SLFFDPERYD LSAVGRVKMN
     LRMDLDCPDT VRILRQEDIL AVVKMLVELR DGRGEIDDID NLGNRRVRSV GELMENQYRI
     GLLRMERAIK ERMSSVEIDT VMPQDLINAK PAAAAVREFF GSSQLSQFMD QTNPLSEITH
     KRRLSALGPG GLTRERAGFE VRDVHPTHYG RICPIETPEG PNIGLINSLA TFARVNKYGF
     IESPYRKIID GKVTTEVIYL SAMEESKHYV AQANSSLDAE GRFTDEFVVC RHAGEVLMAP
     RDHVDLMDVS PKQLVSVAAA LIPFLENDDA NRALMGSNMQ RQAVPLVRAE APFVGTGMES
     IVARDSGAAV SAKRGGIVDQ VDATRIVIRA TEDLDPSKSG VDIYRLQKFQ RSNQSTCINQ
     RPLVHVGDRV EKGNIIADGP STDLGDLALG RNVLVAFMPW NGYNYEDSIL LSERIVADDV
     FTSIHIEEFE VAARDTKLGP EEITRDIPNV AEESLRNLDE AGIIYIGAEV QPGDILVGKI
     TPKGESPMTP EEKLLRAIFG EKASDVRDTS MRMPPGAFGT VVEVRVFNRH GVEKDERAMA
     IEREEIERLA KDRDDEQSIL DRNVYARLTD MLTGKIAVEG PKGFSKGKKL DNTIMGHYPR
     SQWWQFTVED EKLQSEIEAL RRQYDESKEA LQRRFMDKVE KVQRGDEMPP GVMKMVKVFV
     AVKRKIQPGD KMAGRHGNKG VVSRILPIED MPFLEDGTHA DIVLNPLGVP SRMNVGQILE
     THLGWACAGM GKKIGDLVDL YQETGDIFPL RQRIENLMPD NDHNEPVRQY DNESLYKLAL
     QMRKGVSIAT PVFDGAHEAD INMMLEDADL DSSGQVVLYD GRTGEPFDRP VTVGYIYMLK
     LHHLVDDKIH ARSIGPYSLV TQQPLGGKAQ FGGQRFGEME VWALEAYGAA YTLQEMLTVK
     SDDVAGRTKV YEAIVRGDDT FEAGIPESFN VLVKEMRSLA LNVELDDARE LIAQRVLSDT
     TEQ