ID   RPOB_VIBCH              Reviewed;        1341 AA.
AC   Q9KV30;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 2.
DT   03-AUG-2022, entry version 125.
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=VC_0328;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(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=AAF93501.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE003852; AAF93501.1; ALT_INIT; Genomic_DNA.
DR   PIR; F82336; F82336.
DR   RefSeq; NP_229982.2; NC_002505.1.
DR   RefSeq; WP_000263118.1; NZ_LT906614.1.
DR   PDB; 3E7H; X-ray; 1.70 A; A/B=228-329.
DR   PDBsum; 3E7H; -.
DR   AlphaFoldDB; Q9KV30; -.
DR   SMR; Q9KV30; -.
DR   STRING; 243277.VC_0328; -.
DR   DNASU; 2615094; -.
DR   EnsemblBacteria; AAF93501; AAF93501; VC_0328.
DR   GeneID; 57739059; -.
DR   KEGG; vch:VC_0328; -.
DR   PATRIC; fig|243277.26.peg.305; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_3_6; -.
DR   OMA; FMTWEGY; -.
DR   EvolutionaryTrace; Q9KV30; -.
DR   Proteomes; UP000000584; Chromosome 1.
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   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; 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   1: Evidence at protein level;
KW   3D-structure; DNA-directed RNA polymerase; Nucleotidyltransferase;
KW   Reference proteome; Transcription; Transferase.
FT   CHAIN           1..1341
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047992"
FT   STRAND          228..241
FT                   /evidence="ECO:0007829|PDB:3E7H"
FT   HELIX           243..246
FT                   /evidence="ECO:0007829|PDB:3E7H"
FT   STRAND          255..257
FT                   /evidence="ECO:0007829|PDB:3E7H"
FT   STRAND          260..263
FT                   /evidence="ECO:0007829|PDB:3E7H"
FT   HELIX           271..279
FT                   /evidence="ECO:0007829|PDB:3E7H"
FT   STRAND          284..287
FT                   /evidence="ECO:0007829|PDB:3E7H"
FT   HELIX           289..293
FT                   /evidence="ECO:0007829|PDB:3E7H"
FT   STRAND          308..317
FT                   /evidence="ECO:0007829|PDB:3E7H"
FT   HELIX           319..327
FT                   /evidence="ECO:0007829|PDB:3E7H"
SQ   SEQUENCE   1341 AA;  149455 MW;  9C6C824A923295A9 CRC64;
     MVYSYTEKKR IRKDFGTRPQ VLDIPYLLSI QLDSFEKFIE QDPEGQYGLE AAFRSVFPIQ
     SYNGNSELQY VSYRLGEPVF DVKECQIRGV TYSKPLRVKL RLVIFDKDAP AGTVKDIKEQ
     EVYMGEIPLM TENGTFVING TERVIVSQLH RSPGVFFDSD KGKTHSSGKV LYNARIIPYR
     GSWLDFEFDP KDNLYVRIDR RRKLPASIIL RALGKTSAEI LDIFFEKVNF EVKDQTLMME
     LVPERLRGET ATFDIEADGK VYVEKGRRVT ARHIRQLEKD GVNFIEVPVE YIVGKVSAKD
     YVNEATGELI ITANQEISLE ALANLSQAGY KKLEVLFTND LDHGPFMSET LRVDSTTDRI
     SALVEIYRMM RPGEPPTKEA AESLFESLFF SAERYDLSTV GRMKFNSSIG REDAEEQGTL
     DEVDIIEVMK KLISIRNGKG EVDDIDHLGN RRIRSVGEMA ENQFRVGLVR VERAVKERLS
     LGDLDNVMPQ DLINAKPISA AVKEFFGSSQ LSQFMDQNNP LSEVTHKRRI SALGPGGLTR
     ERAGFEVRDV HVTHYGRLCP IETPEGPNIG LINSLSAFAR CNEYGFLETP YRRVVNGVVT
     DEVDYLSAIE EGQFVIAQAN AKLTEEGGFA DELVTARQKG ESGLHPREHV DYMDVATNQV
     VSIAASLIPF LEHDDANRAL MGANMQRQAV PTLRSEKPLV GTGIERNVAV DSGVTAVAKR
     GGVIQSVDAS RIVVKVNEEE LIPGEAGIDI YNLTKYTRSN QNTCINQRPC VMPGEPVARG
     DVLADGPSTD LGELALGQNM RIAFMPWNGY NFEDSILVSE RVVQDDRFTT IHIQELSCVA
     RDTKLGAEEI TADIPNVGEA ALSKLDESGI VYIGAEVKGG DILVGKVTPK GETQLTPEEK
     LLRAIFGEKA SDVKDTSLRV PNSVAGTVID VQVFTRDGVE KDKRALEIEQ MQLKEAKKDL
     TEEFQILEGG LLARVRSVLL AGGYTEAKLG SIERKKWLEQ TLENEELQNQ LEQLAEQYDE
     LKADFDKKFE AKRRKITQGD DLAPGVLKIV KVYLAVKRRI QPGDKMAGRH GNKGVISKIN
     PVEDMPYDEN GQPVDIVLNP LGVPSRMNIG QILEVHLGLA AKGIGDKINQ MIKEQQELAK
     LREFLQKVYD LGDTRQRVDI SELSDEDVRT LAHNLRAGLP VATPVFDGAP ESSIKAMLEL
     ADLPASGQLT LFDGRTGDAF ERPVTVGYMY MLKLNHLVDD KMHARSTGSY SLVTQQPLGG
     KAQFGGQRFG EMEVWALEAY GAAYTLQEML TVKSDDVNGR TKMYKNIVDG NHAMEPGMPE
     SFNVLLKEIR SLGINIELED E