RPOB_NEIG2
ID RPOB_NEIG2 Reviewed; 1392 AA.
AC B4RQW2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=NGK_2420;
OS Neisseria gonorrhoeae (strain NCCP11945).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=521006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCCP11945;
RX PubMed=18586945; DOI=10.1128/jb.00566-08;
RA Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.;
RT "Complete genome sequence of Neisseria gonorrhoeae NCCP11945.";
RL J. Bacteriol. 190:6035-6036(2008).
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; CP001050; ACF31022.1; -; Genomic_DNA.
DR RefSeq; WP_003690105.1; NC_011035.1.
DR AlphaFoldDB; B4RQW2; -.
DR SMR; B4RQW2; -.
DR EnsemblBacteria; ACF31022; ACF31022; NGK_2420.
DR GeneID; 66754280; -.
DR KEGG; ngk:NGK_2420; -.
DR HOGENOM; CLU_000524_4_3_4; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000002564; 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..1392
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000141715"
SQ SEQUENCE 1392 AA; 155719 MW; D0AEA9528D2FF429 CRC64;
MNYSFTEKKR IRKSFAKREN VLEVPFLLAT QIDSYAKFLQ LENAFDKRTD DGLQAAFNSI
FPIVSHNGYA RLEFVYYTLG EPLFDIPECQ LRGITYAAPL RARIRLVILD KEASKPTVKE
VRENEVYMGE IPLMTPSGSF VINGTERVIV SQLHRSPGVF FEHDKGKTHS SGKLLFSARI
IPYRGSWLDF EFDPKDLLYF RIDRRRKMPV TILLKALGYN NEQILDIFYD KETFYLSSNG
VQTDLVAGRL KGETAKVDIL DKEGNVLVAK GKRITAKNIR DITNAGLTRL DVEQESLLGK
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 ADGASTDLGE LALGQNMTIA FMPWNGYNYE
DSILISEKVA ADDRYTSIHI EELNVVARDT KLGAEDITRD IPNLSERMQN RLDESGIVYI
GAEVEAGDVL VGKVTPKGET QLTPEEKLLR AIFGEKASDV KDTSLRMPTG MSGTVIDVQV
FTREGIQRDK RAQSIIDSEL KRYRLDLNDQ LRIFDNDAFD RIERMIVGQK ANGGPMKLAK
GSEITTEYLA GLPSRHDWFD IRLTDEDLAK QLELIKLSLQ QKREEADELY EIKKKKLTQG
DELQPGVQKM VKVFIAIKRR LQAGDKMAGR HGNKGVVSRI LPVEDMPYMA DGRPVDIVLN
PLGVPSRMNI GQILEVHLGW AAKGIGERID RMLKERRKAG ELREFLNKLY NGSGKKEDLD
SLTDEEIIEL ASNLRKGASF ASPVFDGAKE SEIREMLNLA YPSEDPEVEK LGFNDSKTQI
TLYDGRSGEA FDRKVTVGVM HYLKLHHLVD EKMHARSTGP YSLVTQQPLG GKAQFGGQRF
GEMEVWALEA YGAAYTLQEM LTVKSDDVNG RTKMYENIVK GEHKIDAGMP ESFNVLVKEI
RSLGLDIDLE RY
