RPOB_DESPS
ID RPOB_DESPS Reviewed; 1360 AA.
AC Q6AP78;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=DP1117;
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54;
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(2004).
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; CR522870; CAG35846.1; -; Genomic_DNA.
DR RefSeq; WP_011188360.1; NC_006138.1.
DR AlphaFoldDB; Q6AP78; -.
DR SMR; Q6AP78; -.
DR STRING; 177439.DP1117; -.
DR PRIDE; Q6AP78; -.
DR EnsemblBacteria; CAG35846; CAG35846; DP1117.
DR KEGG; dps:DP1117; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_7; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000000602; 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; 1.
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..1360
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000224051"
SQ SEQUENCE 1360 AA; 151635 MW; 000B97C60A1965D6 CRC64;
MERVRKNFAT ADNVLEPPHL ISMQRISYEE FLQIDRAPEE REDVGLQAIL KNIFPINDFN
GLCSLEFLKY KFGEPKYTVQ ECQQRGMSYE IPLKIVVRLI TFDVDEETGV QTIRDMKEQE
VFLGSLPLMT ADGVFVVNGT ERVIVSQLQR SPGLFYSHDN GKSHSSGKLL YSARIIPVRG
SWIDLEFDIK DVLHVRIDRR RKFPVTTLLK ALGYSSEELL REFYPLENVK LSDGKYWVRF
VAEHTAGQRL EFDLVNPQDG EILAKKGRKI SKALCRKAVE AGIEFIEASS ETILGKVLAS
AITLAGAEEP LYPCNTEITE TVLENLAENG INEFETLFMD GVNYSASFSH TLRLDKVITT
AEALLEIYRR LRPSSPPTLE IATTFFENLF FNPDLYDLSE VGRYKINAKL GLKTDIEHRA
LTRDDIIYGV RYLVRLKDNQ GGIDDIDHLG NRRVRTVGEL VENQYRMGLV RMERAIKERM
TLQDVETLMP HDLINPKPIS AAIKEFFGTS QLSQFMDQTN ALSEVTHKRR LSALGPGGLS
RERAGFEVRD VHPTHYGRIC PIETPEGPNI GLIVSLATYA RVNPYGFIET PYRKVENRVI
LDDIRYLSAL EEQKQIIAPA LVALEADHQS ISEGNLIARE EGDVITIGSD NVTYMDVAPN
QMISVAASLV PFLENDDANR ALMGSNMQRQ AVPLLVTAAP LVGTGMERYV ARDSGACLLS
AGDGVVEEVD SNRVVVRYDK PGVDGYDTGV AVYRLTKYKK SNQNTCFTQT PTILPGLKVE
KGTLLADGPG CEAGELALGK NLTVAFMPWR GFNYEDSILI NERLLKEDAY TSIHIDVFET
MARDTKLGKE EITRDIPNVS EDTLRNLDDS GIVRVGAEIK PGDTLVGKVT PKGETVLSPE
EKLLRAIFGE KAQDVKDSSL RVPPGVTGVV IDAKVFSRKG VDKDERSLMI EDLEIERLEG
DKRDELRSLK NGVCRELGEL IAGNTALGDI LDSKGELLIS SGDKIEVVHA IAIGFHRLKD
IDFSGMADCT DRMDAAYERY QKQAEVIAQR YDGIIERQKK GDDLPPGVVK MVKVYVATKR
KLSVGDKMAG RHGNKGVVSR ILPEEDMPYF ANGDTVDIVL NPLGVPSRMN VGQILEVHLG
FAAKNLGAQL EKLAEQYAVE EIKAKLSRVY SDSEYHAIID GKTDAEVIDW AYRHRKGLHM
ATPVFDGAEE AEIRKLLIES GVDKGGQSQL YDGLTGEPFA NLVTVGVMYM LKLHHLVDNK
IHARSTGPYS LVTQQPLGGK AQFGGQRLGE MEVWAMEAYG AAYTLKEFLT VKSDDVEGRT
TMYERIVKGN NFLTTGLPES FHVLVKELQG LCLNMELIEE
