RPOB_VIBVU
ID RPOB_VIBVU Reviewed; 1342 AA.
AC Q8DD20;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=VV1_1211;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
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; AE016795; AAO09671.1; -; Genomic_DNA.
DR RefSeq; WP_011079201.1; NC_004459.3.
DR AlphaFoldDB; Q8DD20; -.
DR SMR; Q8DD20; -.
DR EnsemblBacteria; AAO09671; AAO09671; VV1_1211.
DR KEGG; vvu:VV1_1211; -.
DR HOGENOM; CLU_000524_4_3_6; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000002275; 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 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription;
KW Transferase.
FT CHAIN 1..1342
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047994"
SQ SEQUENCE 1342 AA; 149619 MW; 33D873C489AFC126 CRC64;
MVYSYTEKKR IRKDFGTRPQ VLDIPYLLSI QLDSFDKFIE QDPEGQYGLE AAFRSVFPIQ
SYNGNSELQY VSYRLGEPVF DVKECQIRGV TYSKPLRVKL RLVIFDKDAP AGTVKDIKEQ
EVYMGEIPLM TDNGTFVING TERVIVSQLH RSPGVFFDSD KGKTHSSGKV LYNARIIPYR
GSWLDFEFDP KDNLYVRIDR RRKLPSTIIL RALGKSTEEI LDTFFEKVNF EVKDQTLMME
LVPDRLRGET ATFDIEANGT VYVEKGRRVT ARHIRQLEKE GVDQIEVPVE YIVGKVSSKD
YINEATGEII VAANQEISLE ALAKLSQAGH KQLEVLFTND LDHGPFMSET LRIDSSVDRI
SALVEIYRMM RPGEPPTKEA AEALFESLFF SEERYDLSTV GRMKFNSSIG RDDAEEQGTL
DETDIIEVMK KLIAIRNGKG EVDDIDHLGN RRIRSVGEMA ENQFRVGLVR VERAVKERLS
LGDLDAVMPQ DLINAKPISA AVKEFFGSSQ LSQFMDQNNP LSEVTHKRRI SALGPGGLTR
ERAGFEVRDV HVTHYGRLCP IETPEGPNIG LINSLSAFAR CNEYGFLETP YRRVVDGVVT
DEVDYLSAIE EGQFVIAQAN AKLNEDGTFA DELITARQKG ESGLHPREHV DYMDVATNQV
VSIAASLIPF LEHDDANRAL MGANMQRQAV PTLKAEKPLV GTGIERNVAV DSGVTSVAKR
GGIIQSVDAS RIVVKVNEEE LIPGEAGIDI YNLTKYTRSN QNTCINQRPC VMPGEPVLRG
DVLADGPSTD LGELALGQNM RIAFMPWNGY NFEDSILVSE RVVQEDRFTT IHIQELTCVA
RDTKLGSEEI TADIPNVGES ALSKLDESGI VYIGAEVKGG DILVGKVTPK GETQLTPEEK
LLRAIFGEKA SDVKDTSLRV PNSVSGTIID VQVFTRDGVE KDKRALEIEQ MQLKEAKKDL
TEEFQILEGG LLNRVKAVLL SGGYSEAKLD TTDRKKWLEL TLEDDALQTQ LEQLAEQYDE
LKADFDKKFE TKRRKITQGD DLAPGVLKIV KVYLAVKRRI QPGDKMAGRH GNKGVISKIN
PVEDMPYDEK GQPVDIVLNP LGVPSRMNIG QILEVHLGLA AKGIGDKINQ MVKEQQELAK
FREFLQKVYD LGETRQKVDI ASLSDEEVRT LIGNLRGGLP IATPVFDGAS EASIKELLKL
GGLPESGQLT LFDGRTGDAF ERPVTVGYMY MLKLNHLVDD KMHARSTGSY SLVTQQPLGG
KAQFGGQRFG EMEVWALEAY GAAYTLQEML TVKSDDVNGR TKMYKNIVDG NHAMEPGMPE
SFNVLLKEIR SLGINIELED EQ