RPOB_SYNAS
ID RPOB_SYNAS Reviewed; 1363 AA.
AC Q2LQ87;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=SYNAS_02930;
GN ORFNames=SYN_00064;
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB;
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(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; CP000252; ABC76172.1; -; Genomic_DNA.
DR RefSeq; WP_011416206.1; NC_007759.1.
DR AlphaFoldDB; Q2LQ87; -.
DR SMR; Q2LQ87; -.
DR STRING; 56780.SYN_00064; -.
DR PRIDE; Q2LQ87; -.
DR EnsemblBacteria; ABC76172; ABC76172; SYN_00064.
DR KEGG; sat:SYN_00064; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_7; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000001933; 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..1363
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000237321"
SQ SEQUENCE 1363 AA; 153161 MW; 36F2ADE9AF438F12 CRC64;
MGEFRKNFGR IEEILEVPNL IDIQTRSYET FLQEDVAPEN RKNFGLQGAF KSVFPISDFS
GKCSLEFVSY KIGAVRYDVN ECIQKGMTYA APLKIVVRLV VFDTDRLSDQ KNIRDIKEQE
IYFGEIPLMT EKGTFIVNGT ERVIVSQLHR SPGIFFDHDK GKTLTSGKLI YSARIIPIRG
SWLDLEFDSK DLLYVRIDRR RKMPVTILLK AMGYSTEDLL NYFYDVEHIF CEGENFYAAV
DESLVGHKLY DDIRDINTGE ILFKKGRRIN KVILKRIREQ RVERIKMDVE ELPGRILATD
ILDPETGEVL FHCNEALSAA GIDVVREKGI RELSVINLGE DLSNVSIRDT LLIDRMETPG
DAIIEIYRRL RPSNPPTPDT AQKFFNSLFF ENESYDLSTV GRAKMNYKLR LDVSTDVTVL
RKEDIMAAVK YLIDLKNGVP ECSVDDIDHL GNRRVRSVGE LIENQYRIGL VRMERAIKEK
MSLQDIETMM PHDLVNVKPV SAVVSEFFGS SQLSQFMDQT NPLSEITHKR RLSALGPGGL
TRERAGFEVR DVHPTHYGRI CPVETPEGPN IGLIVSLSTY ARVNEFGFIE TPYRIVKEGR
VLPEVKFLTA IEEENQVIAP ADQPVNHDGS FKGDLISARK GGDFVNVVPS EVNMVDVSPN
QLVSVAATLI PFLEHDDANR ALMGSNMQRQ AVPLMRPEIP LVGTGMERIV ARDSGAVVVA
KRSGIVESVD ASRIVIKCES AEKTDRDTGV DIYTLIKYQR SNQDTCFNQK AIVNKGQRVR
KGDIIADGPA TDNGELALGH NVMVAFMSWG GYNYEDSILV SERIVKEDIY TSIHIEEFET
MARDTKLGKE DITRDIPNVG EEALRNLDDS GIVRMGVSVK SGDILVGKIT PKGETQLSSE
EKLLRAIFGE KASDVRDTSL RVPPGVEGTV IDAKVFTRKG AEKDHRSQYI EDEAIAMLQK
DREDEIRIIT EAVKKEVGTL LQGKQSGAKI VDPKRKKIYL KKGDIITPEI LSEIPLHLWK
EITVADDEET ERAVGQMMAN LYDKIEVVEA YFNEKTEKLK ASDELPPGVI KMVKVYIAIK
RKLQAGDKMA GRHGNKGVLS RILPEEDMPY FKDGRPVDIV LNPLGVPSRM NVGQILETHL
GWAAKGLGEK LNDMLDSYQK GNQLRDELKG IYQSREFEKF VDGATEEETY QFVRKLRRGI
AVSSPVFDGA TESDIRNMLK LANLPSTGQA ILYDGRTGEP FDQEITVGMI YMLKLHHLVD
NKIHARSIGP YSLVTQQPLG GKAQFGGQRL GEMEVWAMEA YGAAYSLQEF LTVKSDDVAG
RTRIYEAIVK GENTSEPGLP ESFNVLVKEL QSLCLDVELI EEE
