ID   RPOB_NEIMB              Reviewed;        1392 AA.
AC   Q59622;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 132.
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=NMB0132;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT RIFAMPICIN RESISTANT.
RC   STRAIN=BNCV / Serogroup B;
RX   PubMed=9222044; DOI=10.1093/jac/39.6.747;
RA   Nolte O.J.;
RT   "Rifampicin resistance in Neisseria meningitidis: evidence from a study of
RT   sibling strains, description of new mutations and notes on population
RT   genetics.";
RL   J. Antimicrob. Chemother. 39:747-755(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF40591.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Z54353; CAA91164.1; -; Genomic_DNA.
DR   EMBL; AE002098; AAF40591.1; ALT_INIT; Genomic_DNA.
DR   PIR; A81236; A81236.
DR   PIR; T30824; T30824.
DR   RefSeq; NP_273190.1; NC_003112.2.
DR   RefSeq; WP_002224771.1; NC_003112.2.
DR   AlphaFoldDB; Q59622; -.
DR   SMR; Q59622; -.
DR   STRING; 122586.NMB0132; -.
DR   PaxDb; Q59622; -.
DR   PRIDE; Q59622; -.
DR   EnsemblBacteria; AAF40591; AAF40591; NMB0132.
DR   KEGG; nme:NMB0132; -.
DR   PATRIC; fig|122586.8.peg.171; -.
DR   HOGENOM; CLU_000524_4_0_4; -.
DR   OMA; FMTWEGY; -.
DR   Proteomes; UP000000425; 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:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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   Antibiotic resistance; DNA-directed RNA polymerase; Nucleotidyltransferase;
KW   Reference proteome; Transcription; Transferase.
FT   CHAIN           1..1392
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047930"
FT   VARIANT         549
FT                   /note="S -> P (rifampicin resistant)"
FT   CONFLICT        2
FT                   /note="N -> S (in Ref. 1; CAA91164)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        28
FT                   /note="L -> I (in Ref. 1; CAA91164)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        224..252
FT                   /note="ILDIFYDKETFYLSSNGVQTDLVADRLKG -> NLGYFLRQRNVLFVFKRCS
FT                   NRFGRRPSES (in Ref. 1; CAA91164)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        284
FT                   /note="N -> L (in Ref. 1; CAA91164)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        350..360
FT                   /note="AYISNTLRTDE -> VISPIPCVRMK (in Ref. 1; CAA91164)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        378
FT                   /note="Missing (in Ref. 1; CAA91164)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        648
FT                   /note="A -> G (in Ref. 1; CAA91164)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        706
FT                   /note="A -> P (in Ref. 1; CAA91164)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        717..718
FT                   /note="VP -> SA (in Ref. 1; CAA91164)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        748..749
FT                   /note="GG -> A (in Ref. 1; CAA91164)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        818
FT                   /note="F -> L (in Ref. 1; CAA91164)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        836..837
FT                   /note="GY -> VN (in Ref. 1; CAA91164)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1190..1192
FT                   /note="YNG -> SR (in Ref. 1; CAA91164)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1201
FT                   /note="A -> S (in Ref. 1; CAA91164)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1244..1246
FT                   /note="DDP -> EDA (in Ref. 1; CAA91164)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1373
FT                   /note="F -> L (in Ref. 1; CAA91164)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1392 AA;  155710 MW;  92AA331A597898F1 CRC64;
     MNYSFTEKKR IRKSFAKREN VLEVPFLLAT QIDSYAKFLQ LENAFDKRTD DGLQAAFNSI
     FPIVSHNGYA RLEFVHYTLG EPLFDIPECQ LRGITYAAPL RARIRLVILD KEASKPTVKE
     VRENEVYMGE IPLMTPSGSF VINGTERVIV SQLHRSPGVF FEHDKGKTHS SGKLLFSARI
     IPYRGSWLDF EFDPKDLLYF RIDRRRKMPV TILLKALGYN NEQILDIFYD KETFYLSSNG
     VQTDLVADRL KGETAKVDIL DKEGNVLVAK GKRITAKNIR DITNAGLTRL DVEPESLLGK
     ALAADLIDSE TGEVLASAND EITEELLAKF DINGVKEITT LYINELDQGA YISNTLRTDE
     TAGRQAARVA IYRMMRPGEP PTEEAVEQLF NRLFFSEDSY DLSRVGRMKF NTRTYEQKLS
     EAQQNSWYGR LLNETFAGAA DKGGYVLSVE DIVASIATLV ELRNGHGEVD DIDHLGNRRV
     RSVGELTENQ FRSGLARVER AVKERLNQAE SENLMPHDLI NAKPVSAAIK EFFGSSQLSQ
     FMDQTNPLSE VTHKRRVSAL GPGGLTRERA GFEVRDVHPT HYGRVCPIET PEGPNIGLIN
     SLSVYARTND YGFLETPYRR VIDGKVTEEI DYLSAIEEGR YVIAQANADL DSDGNLIGDL
     VTCREKGETI MATPDRVQYM DVATGQVVSV AASLIPFLEH DDANRALMGA NMQRQAVPCL
     RPEKPMVGTG IERSVAVDSA TAIVARRGGV VEYVDANRVV IRVHDDEATA GEVGVDIYNL
     VKFTRSNQST NINQRPAVKA GDVLQRGDLV ADGASTDFGE LALGQNMTIA FMPWNGYNYE
     DSILISEKVA ADDRYTSIHI EELNVVARDT KLGAEDITRD IPNLSERMQN RLDESGIVYI
     GAEVEAGDVL VGKVTPKGET QLTPEEKLLR AIFGEKASDV KDTSLRMPTG MSGTVIDVQV
     FTREGIQRDK RAQSIIDSEL KRYRLDLNDQ LRIFDNDAFD RIERMIVGQK ANGGPMKLAK
     GSEITTEYLA GLPSRHDWFD IRLTDEDLAK QLELIKVSLQ QKREEADELY EIKKKKLTQG
     DELQPGVQKM VKVFIAIKRR LQAGDKMAGR HGNKGVVSRI LPVEDMPYMA DGRPVDIVLN
     PLGVPSRMNI GQILEVHLGW AAKGIGERID RMLKEQRKAG ELREFLNRLY NGSGKKEDLD
     ALTDEEIIEL ASNLRKGASF ASPVFDGAKE SEIREMLNLA YPSDDPEVEK LGFNDSKTQI
     TLYDGRSGEA FDRKVTVGVM HYLKLHHLVD EKMHARSTGP YSLVTQQPLG GKAQFGGQRF
     GEMEVWALEA YGAAYTLQEM LTVKSDDVNG RTKMYENIVK GEHKIDAGMP ESFNVLVKEI
     RSLGLDIDLE RY