RPOB_PARL1
ID RPOB_PARL1 Reviewed; 1362 AA.
AC A7HWQ4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Plav_2729;
OS Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Parvibaculaceae; Parvibaculum.
OX NCBI_TaxID=402881;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-1 / DSM 13023 / NCIMB 13966;
RX PubMed=22675581; DOI=10.4056/sigs.2215005;
RA Schleheck D., Weiss M., Pitluck S., Bruce D., Land M.L., Han S.,
RA Saunders E., Tapia R., Detter C., Brettin T., Han J., Woyke T., Goodwin L.,
RA Pennacchio L., Nolan M., Cook A.M., Kjelleberg S., Thomas T.;
RT "Complete genome sequence of Parvibaculum lavamentivorans type strain (DS-
RT 1(T)).";
RL Stand. Genomic Sci. 5:298-310(2011).
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; CP000774; ABS64337.1; -; Genomic_DNA.
DR RefSeq; WP_012111652.1; NC_009719.1.
DR AlphaFoldDB; A7HWQ4; -.
DR SMR; A7HWQ4; -.
DR STRING; 402881.Plav_2729; -.
DR EnsemblBacteria; ABS64337; ABS64337; Plav_2729.
DR KEGG; pla:Plav_2729; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_5; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000006377; 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; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1362
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000073239"
SQ SEQUENCE 1362 AA; 151816 MW; 3853A205F2E9FBB0 CRC64;
MTQSFTGRKR VRKVFGHIPQ IAEMPNLIEV QKYSYDQFLQ VDEPTGGREE QGLQAVFKSV
FPISDFSESS TLEFVNYEFE TPKYDVEECQ QRGMTFAAPL KVTLRLIVFE VDEDTGAKSV
KDIKEQDVYM GDMPLMTENG TFVINGTERV IVSQMHRSPG VFFDHDKGKT HSSGKLLFAA
RVIPYRGSWL DFEFDAKDIV FVRIDRRRKL PVTTLLYALG LDSEEILSTF YNSVTFTKVK
QGWRVPFNAD RYRGAKPERD LIDAKTGKVV VEAGRKVTPR LAKKLAEEGL KELLVQDEDI
HTRYLAQEIV NMETGEIFAE AGDEITPELL EALVEAGHTD IITLDIDHVN TGAFIRNTLA
VDKCTNREQA LIDIYRVMRP GEPPTADTAE ALFKSLFFDA ERYDLSAVGR VKMNMRLDLD
VSDTVRVLRK EDILAVIKTL VGLRDGKGEI DDIDNLGNRR VRSVGELMEN QYRVGLLRME
RAIKERMSSV DIDTVMPHDL INAKPAAAAV REFFGSSQLS QFMDQTNPLS EITHKRRLSA
LGPGGLTRER AGFEVRDVHP THYGRICPIE TPEGPNIGLI NSLATFARVN KYGFIESPYR
RVKGGKLADD IVYLSAMEES RYRIAQANVA IGKKGEIEGE LVNCRIDGDF EMVPPDQVDF
VDVSPKQIVS VAAALIPFLE NDDANRALMG SNMQRQAVPL IRSEAPLVGT GMEEVVARDS
GAAIGARRTG VVDQVDATRI VIRATEEVDS SKSGVDIYNL RKFQRSNQNT CINQRPLVRV
GDQVKKGDII ADGPSTELGD LALGRNVLVA FMPWNGYNFE DSILISERIV RDDVFTSIHI
EEFEVMARDT KLGPEEITRD IPNVGEEALK NLDEAGIVYI GAEVNPGDIL CGKITPKGES
PMTPEEKLLR AIFGEKASDV RDTSLRLPPG VQGTVVEVRV FNRHGIDKDE RAMAIEREEI
ERLAKDRDDE FGILDRNVYG RLSEILLGKQ IASGPKGMEA DAKVTQANLD DLSHGQWWQI
ALKNEKAQSE IEALKKQYDE SKERLEARFA DKVDKLQRGD ELPPGVMKMV KVFVAVKRKL
QTGDKMAGRH GNKGVISRIV PMEDMPYLDD GQPVDIVLNP LGVPSRMNVG QILETHLGWA
CAGLGKKIEV ALDAYHRENK PKELKDLVKQ IYGDDPTVAS LDEEQLVEMA GNLTNGVPIA
TPVFDGAREP EIVEMLELAG LDRSGQVTLH DGRTGEPFDR KVTVGYIYML KLHHLVDDKI
HARSIGPYSL VTQQPLGGKA QFGGQRFGEM EVWALEAYGA AYTLQEMLTV KSDDVAGRTK
VYEAIVRGDD TFEAGIPESF NVLVKEMRSL GLNVELLTPA AN