RPOB_SULNB
ID RPOB_SULNB Reviewed; 1385 AA.
AC A6Q6I2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=SUN_0131;
OS Sulfurovum sp. (strain NBC37-1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Sulfurovaceae; Sulfurovum; unclassified Sulfurovum.
OX NCBI_TaxID=387093;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBC37-1;
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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; AP009179; BAF71091.1; -; Genomic_DNA.
DR RefSeq; WP_011979824.1; NC_009663.1.
DR AlphaFoldDB; A6Q6I2; -.
DR SMR; A6Q6I2; -.
DR STRING; 387093.SUN_0131; -.
DR PRIDE; A6Q6I2; -.
DR EnsemblBacteria; BAF71091; BAF71091; SUN_0131.
DR KEGG; sun:SUN_0131; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_7; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000006378; 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; -; 2.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 2.
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..1385
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000329191"
SQ SEQUENCE 1385 AA; 156770 MW; 6B28588BCAD463EB CRC64;
MLNSLHSGNR LRVDFSKTPR EIEIPNLLQL QQKSYENFLM LGERDRKHST LERVFRSAFP
IHDQQNRLTL TYKNSEIIKP KYTVRECMER GLTYSVSLKM NIALTIWNRD EKTGEKLDPK
EIKEQAVFVR DIPLMTERTS FVVNGVERVI VNQLHRSPGV IFKEEESTTA GHKLLYSAQI
IPDRGSWLYF EYDAKDILYA RINKRRKIPV TILFRALDYT KEDIVKLFYP TKEISIKDNR
FLVKFDPSDF SGRAEYDVKD MDGNVIVNAG KRLTKKKAQQ LIENGLEWIE YPLEMLMERH
LATAVIDQES GEVLYDVVAP LDETKLKKMI EQGIESIEII NDLAEGTDKS IINAFIADNE
SLRLLKQTEE IDDENVLSAI RIYKVMRPGE PVTPEAAKSF LRQLFFDPER YDLTEVGRMK
MNHKLGLDIP QYATVLTAED LINTVKYLIK VKNGHGHIDD RDHLGNRRIR AIGELLGNEL
HNGLVKMQKA IKDKMTTISG TLDELMPHDL VNSKMITNTI LEFFSSGQLS QFMDQTNPLS
EVTHKRRLSA LGEGGLVKER AGFEVRDVHP THYGRICPIE TPEGQNIGLI NTLATYSKVN
EHGFIEAPYK VVKDAQVTDE IVYITATQEE DKCIAPASTK VDENGKIVED LIETRLNGNI
ELNEAKRVDL IDISPLMISG SAAALIPFLE HDDANRALMG SNMQRQAVPL LKTDAPVVGT
GMEAIVSRDA WEAVKAKRAG KVEKVDAKNI YIMGEDETGV FIDHYPLEKN MRTNQNTTFT
QTPIVKLGDV IEVGQVIADG ANMDQGELAI GKNIMVAFMP WYGYNYEDAI IVSEKIIRED
TFTSVHTYEK EVEARELKHG TEEITRDIPN IREDELLHLD ESGIVQLGTY VKPGMILVGK
VSPKGEIKPT PEERLLRAIF GEKAGHVVNK SLYCPASMEG VVVDIKVFTK KGYEKDARAI
QAYEEEKAIL DSDHHDQLLM IDREEILRIA HYLSGQELAK DVTIGDKEYK AGSKIDEETI
KGVNRFALRG VVQSYSDDVQ NEYEALKNYF LKQKKRLKNE HEEKLSILEK DDILPSGVTK
LVKIYIATKR KLKVGDKMAG RHGNKGIVSN IVPEIDMPYM EDGRPVEIIL NPLGVPSRMN
IGQILEVHLG LVGMRLGEQI QEMFDNKTAD FIKELRAKMI EIADVAKLMN AKEVLSQMSD
EELLAYGRDW SRGVKFAAPV FEGTNQTEFD KLFELAKIES DGKMTLYDGK TGEKMIERVN
VGYMYMLKLH HLVDEKVHAR STGPYSLVTQ QPVGGKALFG GQRFGEMEVW ALEAYGASHI
LKEMLTIKSD DVEGRARAYR ALTKGESVPA SGVPETMFVL TKELQALGLD AELYESKKEV
ESEDE
