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RPOC_OPITP
ID   RPOC_OPITP              Reviewed;        1384 AA.
AC   B1ZPB7;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE            Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322};
DE   AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE   AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
GN   Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322}; OrderedLocusNames=Oter_0231;
OS   Opitutus terrae (strain DSM 11246 / JCM 15787 / PB90-1).
OC   Bacteria; Verrucomicrobia; Opitutae; Opitutales; Opitutaceae; Opitutus.
OX   NCBI_TaxID=452637;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11246 / JCM 15787 / PB90-1;
RX   PubMed=21398538; DOI=10.1128/jb.00228-11;
RA   van Passel M.W., Kant R., Palva A., Copeland A., Lucas S., Lapidus A.,
RA   Glavina del Rio T., Pitluck S., Goltsman E., Clum A., Sun H., Schmutz J.,
RA   Larimer F.W., Land M.L., Hauser L., Kyrpides N., Mikhailova N.,
RA   Richardson P.P., Janssen P.H., de Vos W.M., Smidt H.;
RT   "Genome sequence of the verrucomicrobium Opitutus terrae PB90-1, an
RT   abundant inhabitant of rice paddy soil ecosystems.";
RL   J. Bacteriol. 193:2367-2368(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_01322}.
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_01322};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01322};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC       Note=Binds 1 Zn(2+) ion per subunit; 2 are expected compared to other
CC       organisms. {ECO:0000305};
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_01322}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01322}.
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DR   EMBL; CP001032; ACB73522.1; -; Genomic_DNA.
DR   RefSeq; WP_012373060.1; NC_010571.1.
DR   AlphaFoldDB; B1ZPB7; -.
DR   SMR; B1ZPB7; -.
DR   STRING; 452637.Oter_0231; -.
DR   PRIDE; B1ZPB7; -.
DR   EnsemblBacteria; ACB73522; ACB73522; Oter_0231.
DR   KEGG; ote:Oter_0231; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_0; -.
DR   OMA; YRNIRVE; -.
DR   OrthoDB; 4421at2; -.
DR   Proteomes; UP000007013; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.274.100; -; 1.
DR   Gene3D; 4.10.860.120; -; 1.
DR   HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR012754; DNA-dir_RpoC_beta_prime_bact.
DR   InterPro; IPR000722; RNA_pol_asu.
DR   InterPro; IPR006592; RNA_pol_N.
DR   InterPro; IPR007080; RNA_pol_Rpb1_1.
DR   InterPro; IPR007066; RNA_pol_Rpb1_3.
DR   InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR   InterPro; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   PANTHER; PTHR19376; PTHR19376; 1.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR   Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR   SMART; SM00663; RPOLA_N; 1.
DR   TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW   Zinc.
FT   CHAIN           1..1384
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000353398"
FT   BINDING         81
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         472
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         474
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         476
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1384 AA;  152789 MW;  84B0D78CDCB261D7 CRC64;
     MSIQPSEVAA SSARTDTREA LGIEESAFDC VSITVASPET IRKWSKGEVK NPETINYRTF
     KPEPGGLFCQ KIFGPVRDYE CACGKYKRIK YKDVVCDRCG VEVTIARVRR ERMGHIELAV
     PVAHIWFLKS MPSRLGLLLD MTARSLERVI YYENYMVIDP GKTPLEPHQL LTDTEYRQAI
     DEYGEDSFVA KMGAEAVRDA LVKTDLEATV AELQEQMRAT KSKQIKKKLS KRLKVIQGFI
     HSKSRPEWMV LEVLPVIPPD LRPLVPLEGG RFATSDLNDL YRRVINRNNR LRNLMQLKTP
     DVIIHNEKRM LQEAVDALFD NGRHGRPVTG AGNRPLKSLS DMLKGKQGRF RQNLLGKRVD
     YSGRSVIVIG PELKLHQCGL PKKMALVLFE PFIIRRLKEL GFVHTVRGAR KMIEKKSPEV
     WDILEEVTKG HPVLLNRAPT LHRLSIQAFE PVLIEGEAIR VHPLVCTAYN ADFDGDQMAV
     HVPLSLEAIM ECKLLMMATS NIFSPSSGKP ILTPSQDIVL GAYYLTVEPR KKPAKDERVP
     LLSGLQEVLY AVADGAMKKH DWVEVPNPDH GRETIFGNKE KKVLRTTVGR VIFNQIWPAG
     LGFVNFPVPK SKLGDLILNT HKLTGNQATV ETLDRLKELG FTTAMQAGIS IGIDDMIIPE
     AKKDIVAETR KKIAEVEAQF NKGIITEGER KNKVIDLWTG TTDRIAKEVF AKLESNEGRN
     EVNPVYIMMD SGARGNKQQV RQLCGTRGLM AKPSGEIIER PILSSFREGL TVLEYFISTH
     GARKGLADTA LKTADAGYLT RKLCDVAMDV IIAEDDCGSR DGVWKKAIFE GDDEIVSLRE
     RIVGRFSSDD VFNPINPSEI LVGSGELITE EIATRVDELG IERVKVMSPL TSTAQHGIDG
     KSYGINPATG KVAKVGDSVG IIAAQSIGEP GTQLTMRTFH IGGVASGGFK TPEIKVRASG
     TVRYRGLRLV ETADGGSIVL NKTGTIQIVD AEEKELETYN IVVGSFLHVG DGEQIQKGAI
     LAQWDPYNIP VLSEKGGTLA FKDMIPGVTV KRELDESSGR IATVVIEHKE DLNPQIEIRD
     PKGKPLAAYS IPVGAQIAVN EGDIIQPGAL LAKTPRQASK TKDITGGLPR VAELFEARRP
     KDAAEMSRID GIVSFEGTVR GKRKLVVKND DTAQEEEHLI ATGKHIIVQP GDVVHKGQHL
     TEGAADPHEI LEILGPSALY DFLISQVQEV YRLQGVAIND KHIEIIIRQM LRKVRITDPG
     DTENFWGEQV DRAQFLAENR RIEEAGGKPA EAEPILLGIT KASLETESFI SAASFQETTR
     VLTDASTLGK VDMLKGFKEN VIMGHLIPAG TGLPKYKNLK ITLPFGADLP VEPEQPAPAA
     TETA
 
 
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