RPOB_RHOPT
ID RPOB_RHOPT Reviewed; 1374 AA.
AC B3QC00;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Rpal_3687;
OS Rhodopseudomonas palustris (strain TIE-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=395960;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TIE-1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA Newman D.K., Roden E., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL Submitted (MAY-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; CP001096; ACF02187.1; -; Genomic_DNA.
DR RefSeq; WP_011158811.1; NC_011004.1.
DR AlphaFoldDB; B3QC00; -.
DR SMR; B3QC00; -.
DR EnsemblBacteria; ACF02187; ACF02187; Rpal_3687.
DR GeneID; 66894354; -.
DR KEGG; rpt:Rpal_3687; -.
DR HOGENOM; CLU_000524_4_0_5; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR BioCyc; RPAL395960:RPAL_RS18240-MON; -.
DR Proteomes; UP000001725; 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; -; 1.
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..1374
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000141728"
SQ SEQUENCE 1374 AA; 153599 MW; 1110C67B5CA5CF48 CRC64;
MAQQTFTGRK RVRKFFGHIR EVAEMPNLIE VQKASYDQFL MVAEPPGGRP DEGLQAVFRS
VFPISDFSNA SMLEFVRYEF EPPKYDVDEC RQRGMTYAAP LKVTLRLIVF DIDEETGARS
VKDIKEQDVY MGDIPLMTMN GTFIVNGTER VIVSQMHRSP GVFFDHDKGK THSSGKLLFA
ARIIPYRGSW LDIEFDAKDI VYARIDRRRK LPVTSLMFAL GLDGEEILST FYNKILYKRT
KEGWRVPFDV NRFRGYSTVN DLIDADTGKV VLEAGKKLTV RAARQLQEKG LKALRMSDEE
LVGNYLAEDL VNPKTGEIYA EAGEEITDKT LKMLNEQGYK ELPLLDIDHV NVGPYIRNTL
NADKNMTRED ALFDIYRVMR PGEPPTLDSA QNMFQSLFFD AERYDLSAVG RVKMNMRLDL
DAPDTHRTLR KEDILAVIKT LVGLRDGKGE IDDIDHLGNR RVRSVGELME NQYRIGLLRM
ERAIKERMSS VDIDTVMPQD LINAKPAAAA VREFFGSSQL SQFMDQTNPL SEITHKRRLS
ALGPGGLTRE RAGFEVRDVH PTHYGRICPI ETPEGPNIGL INSLATFARV NKYGFVETPY
RKVKEGRVTD EVVYLSAMEE GRYAVAQANV SLDAKGKFTD DLVVCRAGGT RDVVPMPADQ
VDYMDVSPKQ LVSVAAALIP FLENDDANRA LMGSNMQRQA VPLVRAEAPF VGTGMEGVVA
RDSGAAIAAR RTGIIDQIDA TRIVIRATED LDPTKSGVDI YRLMKYQRSN QSTCINQRPL
VKVGDHVKKG DIIADGPSTD LGELALGRNV LVAFMPWNGY NFEDSILLSE RIVKEDVFTS
IHIEEFEVMA RDTKLGPEEI TRDIPNVSEE ALKNLDEAGI VYIGAEVRAG DILVGKITPK
GESPMTPEEK LLRAIFGEKA SDVRDTSLRV PPGVQGTIVE VRVFNRHGVD KDERALAIER
EEIERLAKDR DDEQAILDRN VYGRLADLLD GRQGIAGPKG FKKDTKITRA VLEEYPKSQW
WLFAAPNDKL MAEIEAMRKQ YDESKKGLEQ RFLDKVEKLQ RGDELPPGVM KMVKVFVAVK
RKIQPGDKMA GRHGNKGVVS KIVPIEDMPF LEDGTHADIV LNPLGVPSRM NVGQILETHL
GWACAGLGKR IGETIDAYYQ SQDLKPLRET LRKIYGEDET IKSLDDGELL ELGRNLSHGV
PIATPVFDGA KEADIEEMLK LAGFDASGQS TVYDGRTGDQ FDRRVTVGYI YMLKLHHLVD
DKIHARSIGP YSLVTQQPLG GKAQFGGQRF GEMEVWALEA YGAAYTLQEM LTVKSDDVAG
RTKVYEAIVR GDDTFEAGIP ESFNVLVKEM RSLGLNVDLH NSKLAAPPPA EAAE
