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RPOC_PORGI
ID   RPOC_PORGI              Reviewed;        1433 AA.
AC   Q7MX26;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=PG_0395;
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=242619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83;
RX   PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA   Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA   Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA   Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA   Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA   Fraser C.M.;
RT   "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT   gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(2003).
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 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01322};
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; AE015924; AAQ65600.1; -; Genomic_DNA.
DR   RefSeq; WP_005873811.1; NC_002950.2.
DR   AlphaFoldDB; Q7MX26; -.
DR   SMR; Q7MX26; -.
DR   STRING; 242619.PG_0395; -.
DR   PRIDE; Q7MX26; -.
DR   EnsemblBacteria; AAQ65600; AAQ65600; PG_0395.
DR   KEGG; pgi:PG_0395; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_10; -.
DR   OMA; YRNIRVE; -.
DR   OrthoDB; 4421at2; -.
DR   Proteomes; UP000000588; 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; 2.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 2.
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..1433
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000067776"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         81
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         473
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         475
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         477
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         815
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         889
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         896
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         899
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1433 AA;  160260 MW;  2709B8BA7782BE44 CRC64;
     MAFRKENKIK NNFSKIRITL ASPEEILENS FGEVLKPETI NYRTYKPERD GLFCERIFGP
     VKDFECHCGK YKRIRYRGIV CDRCGVEVTE KKVRRERMGH IHLVVPVAHI WYFRSLPNKI
     GYLLGLPTKK LDAIIYYERY VVIQPGVAEG LSQLDLLSEE EYLDKLDEIE RTHKGNQNLE
     DTNPDKFIAK IGAEAIYDLL CRVDLDSISY ELRDRANTDG SQQRKTEALK RLQVVESFRA
     SKGVNRPEWM VMKVIPVIPP DLRPLVPLDG GRFATSDLND LYRRVIIRNN RLKRLIEIKA
     PEVILRNEKR MLQEAVDSLF DNSRKSSAVK SDNNRPLKSL SDSLKGKQGR FRQNLLGKRV
     DYSARSVIVV GPELKMHECG LPKDMAAELY KPFIIRKLIE RGIVKTVKSA KKIVDRKEPV
     IWDILEYVMK GHPVLLNRAP TLHRLGIQAF QPKLIEGKAI QLHPLSCTAF NADFDGDQMA
     VHLPLSNEAI LEAQLLMLAS HNILNPANGA PITVPSQDMV LGLYYITKLR PNTKGHGLIF
     YGPEEATIAY NEGKVDIHAP IKVYVEDYEN GELVRRMVET SVGRLMVNEY VPKKVGYVNE
     VLGKKALRDI IGSVIKICGV ATTAKFLDDI KNLGYYMAFK GGLSFNLADV LIPDEKDQLI
     QEGYTAVEQI MQDYSMGFIT FNERYNQIID TWTHINGRLS NVLIKQLSSD NDGFNSVFMM
     MDSGARGSKE QIRQLSGMRG LMAKPQKSGA EGGQIIENPI LSNFKEGLSV LEYFISTHGA
     RKGLADTALK TADAGYLTRR LVDVSHDVII TEEDCGTLRG LLTTELKQNE DVVASLYERI
     LGRVSVHDII HPTTGDIIVR AGEEIREQAA QIIEDSPIEA VEIRSVLTCE SKKGVCAKCY
     GRNLATNRMV QRGEVVGVIA AQSIGEPGTQ LTLRTFHVGG IASNVATENS LLSKYDGILE
     FEELRAVDVT DESHQVVVSR MTELRIADPN TGIILANHNI PYGAKLFFRQ GDAVKKGDKI
     IEWDPFNAVI VSEVAGTLSF EGVVENVTFK MESDETTGLK EKIIIESKDK TMAPYARIID
     ENGEMLKNYS LPMGAHVVKD DGDTVKVGEI LVKIPRSVGK AGDITGGLPR VTELFEARNP
     SNPAIVSEID GEIGFGKLKR GNREITVTSK LGEEKKYLIP LSKQLLVQEN DFVRAGTPLS
     DGAITPADIL AIKGPTAVQE YIVNEVQDVY RLQGVKINDK HFEVIVRQMM RKVEIVDPGD
     TLFLEQQVVD KFEVMEENDR IWGKKVVIDA GDSQVLKAGQ IVTARKLRDE NSMLKRKDLK
     IVKVRDAKSA TASQILQGIT RAALQTKSFM SAASFQETTK VLNEAAICGK TDYLEGLKEN
     VICGHLIPAG TGLRDYEKLV VMHRDDYEKA TAERKSFLSV PTAEPAMEEA PSE
 
 
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