RPOB_ALIFM
ID RPOB_ALIFM Reviewed; 1342 AA.
AC B5FC88;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=VFMJ11_2530;
OS Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=388396;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ11;
RA Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT "Complete sequence of Vibrio fischeri strain MJ11.";
RL Submitted (AUG-2008) 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; CP001139; ACH66489.1; -; Genomic_DNA.
DR RefSeq; WP_012533765.1; NC_011184.1.
DR AlphaFoldDB; B5FC88; -.
DR SMR; B5FC88; -.
DR EnsemblBacteria; ACH66489; ACH66489; VFMJ11_2530.
DR KEGG; vfm:VFMJ11_2530; -.
DR HOGENOM; CLU_000524_4_0_6; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000001857; Chromosome I.
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; -; 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..1342
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000141748"
SQ SEQUENCE 1342 AA; 149996 MW; 089DA07FD257B374 CRC64;
MVYSYTEKKR IRKDFGKRPQ VLDIPYLLSI QLDSFTKFIE QDPEGQYGLE AAFRSVFPIQ
SYNGNSKLEY VSYNLREPEF DVKECQIRGV TYSAPLRVKL RLVVYDKDAP ANTVKDIKEQ
EVYMGEIPLM TDNGTFVING TERVIVSQLH RSPGVFFDSD KGKTHSSGKV LYNARVIPYR
GSWLDFEFDP KDNLFVRIDR RRKLPATIIL RALNKTTEEI LDLFFDKVVF EVKDQTLMME
LLPERLRGET ATFDIEANGK VYVEAGRRIT ARHIRQLTKD DITHIEVPVD YIVGKVASHD
YVNEDTGEII IAANQEFSLE DLANLSQAGY KKIEVLFTND LDHGAYISDT LRADSTVDRL
SALVEIYRMM RPGEPPTKEA AEALFESLFF SEERYDLSTV GRMKFNSSIG RDNDEGAGVL
DETDIIEVMR KLIDIRNGIG EVDDIDHLGN RRIRSVGEMA ENQFRVGLVR VERAVRERLS
LGDLDAIMPQ DLINAKPISA AVKEFFGSSQ LSQFMDQNNP LSEVTHKRRI SALGPGGLTR
ERAGFEVRDV HATHYGRLCP IETPEGPNIG LINSLSAFAQ CNEYGFLETP YRRVVDGQVT
DQVDYLSAIE EGTFVIAQAN AVLTEEGTFA DELIIARQKG ESGLHPREHI QYMDVATNQV
VSVAASLIPF LEHDDANRAL MGANMQRQAV PTLKADKPLV GTGIERNVAV DSGVTAVAKR
GGVVQSVDAS RIVIKVNEEE LVPGEAGIDI YNLTKYTRSN QNTCINQRPT VLPGEPVTRG
DVLADGPSTD LGELALGQNM RIAFMPWNGY NFEDSILVSE RVVQEDRFTT IHIQELSCVA
RDTKLGSEEI TADIPNVGEA ALSKLDESGI VYIGAEVKGG DILVGKVTPK GETQLTPEEK
LLRAIFGEKA SDVKDSSLRV PNSVSGTIID VQVFTRDGVE KDKRALEIEQ MQLKEAKKDI
TEEFQILEGG LLARVRTLLV AAGVSEVKLD AMDRKQWLEI TLDDEAQQNQ LEQLAEQYDE
LKAEFDKKFE TKRRKITQGD DLAPGVLKIV KVYLAVKRRI QPGDKMAGRH GNKGVISKIN
PVEDMPYDEK GQPVDIVLNP LGVPSRMNIG QILEVHMGLA AKGVGDKINQ MLKEQQELHK
FRNFLQKVYD LGETRQEVDI AALSDDEVRT LIKNLRGGLP IATPIFDGAP EASIKELLKL
VDLPESGQLK LFDGRTGDAF ERPVTVGYMY MLKLNHLVDD KMHARSTGSY SLVTQQPLGG
KAQFGGQRFG EMEVWALEAY GAAYTLQEML TVKSDDVNGR TKMYKNIVDG DHRMEPGMPE
SFNVLLKEIR SLGINIELED EE
