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RPOC_NEIG2
ID   RPOC_NEIG2              Reviewed;        1391 AA.
AC   B4RQW3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=NGK_2421;
OS   Neisseria gonorrhoeae (strain NCCP11945).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=521006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCCP11945;
RX   PubMed=18586945; DOI=10.1128/jb.00566-08;
RA   Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.;
RT   "Complete genome sequence of Neisseria gonorrhoeae NCCP11945.";
RL   J. Bacteriol. 190:6035-6036(2008).
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; CP001050; ACF31023.1; -; Genomic_DNA.
DR   RefSeq; WP_003690305.1; NC_011035.1.
DR   AlphaFoldDB; B4RQW3; -.
DR   SMR; B4RQW3; -.
DR   PRIDE; B4RQW3; -.
DR   EnsemblBacteria; ACF31023; ACF31023; NGK_2421.
DR   GeneID; 66754282; -.
DR   KEGG; ngk:NGK_2421; -.
DR   HOGENOM; CLU_000524_3_1_4; -.
DR   OMA; YRNIRVE; -.
DR   OrthoDB; 4421at2; -.
DR   Proteomes; UP000002564; 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; 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; Transcription; Transferase; Zinc.
FT   CHAIN           1..1391
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_1000141786"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         87
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         462
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         464
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         466
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         816
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         890
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         897
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         900
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1391 AA;  153796 MW;  5E4A8FA4C6F1BB89 CRC64;
     MNLLNLFNPL QTAGMEEEFD AIKIGIASPE TIRSWSYGEV KKPETINYRT FKPERDGLFC
     AKIFGPVKDY ECLCGKYKRL KFKGVTCEKC GVEVTLSKVR RERMGHIELA APVAHIWFLK
     SLPSRLGMVL NMTLRDIERV LYFEAFVVTD PGMTPLQRRQ LLTEDDYYNK LDEYGDDFDA
     KMGAEGIREL LRTLDVAGEI EILRQELEST GSDTKIKKIA KRLKVLEAFH RSGMKLEWMI
     MDVLPVLPPD LRPLVPLDGG RFATSDLNDL YRRVINRNNR LKRLLELHAP DIIVRNEKRM
     LQEAVDSLLD NGRRGKAMTG ANKRPLKSLA DMIKGKGGRF RQNLLGKRVD YSGRSVITVG
     PYLRLHQCGL PKKMALELFK PFIFHKLEKQ GLASTVKAAK KLVEQEVPEV WDILEEVIRE
     HPIMLNRAPT LHRLGIQAFE PILIEGKAIQ LHPLVCAAFN ADFDGDQMAV HVPLSLEAQM
     EARTLMLASN NVLSPANGEP IIVPSQDIVL GLYYMTRDRI NAKGEGSLFA DVKEVHRAYH
     TKQVELGTKI TVRLREWVKN EAGEFEPVVN RYETTVGRAL LSEILPKGLP FEYVNKALKK
     KEISKLINAS FRLCGLRDTV IFADHLMYTG FGFAAKGGIS IAVDDMEIPK EKAALLAEAN
     AEVKEIEDQY RQGLVTNGER YNKVVDIWGR AGDKIAKAMM DNLSKQKVID RDGNEVDQES
     FNSIYMMADS GARGSAAQIK QLSGMRGLMA KPDGSIIETP ITSNFREGLT VLQYFIATHG
     ARKGLADTAL KTANSGYLTR RLVDVTQDLV VVEDDCGTSD GFVMKAVVQG GDVIEALRDR
     ILGRVTASDV VDPSSGETLV EAGTLLTEKL VDMIDQSGVD EVKVRTPITC KTRHGLCAHC
     YGRDLARGKL VNAGEAVGVI AAQSIGEPGT QLTMRTFHIG GAASRAAAAS QVEAKSNGTA
     RFSSQMRYVA NNKGELVVIG RSCEVVIHDD IGRERERHKV PYGAILLVQD GMAIKAGQTL
     ATWDPHTRPM ITEHAGMVKF ENMEEGVTVA KQTDDVTGLS ALVVIDGKRR SSSASKLLRP
     TVKLLDENGV EICIPGTSTP VSMAFPVGAV ITVREGQEIG KGDVLARIPQ ASSKTRDITG
     GLPRVAELFE ARVPKDAGML AEITGTVSFG KETKGKQRLI ITDVDGVAYE TLISKEKQIL
     VHDGQVVNRG ETIVDGAVDP HDILRLQGIE ALARYIVQEV QEVYRLQGVK ISDKHIEVII
     RQMLRRVNIA DAGETGFITG EQVERGDMMA ANEKALEEGK EPARYENILL GITKASLSTD
     SFISAASFQE TTRVLTEAAI MGKQDELRGL KENVIVGRLI PAGTGLTYHR SRHQQWQGVE
     QETAETQVTD E
 
 
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