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NAPD_ECO57
ID   NAPD_ECO57              Reviewed;          87 AA.
AC   P0A9I6; P33938;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Chaperone NapD {ECO:0000255|HAMAP-Rule:MF_02200};
DE   AltName: Full=NapA signal peptide-binding chaperone NapD {ECO:0000255|HAMAP-Rule:MF_02200};
GN   Name=napD {ECO:0000255|HAMAP-Rule:MF_02200};
GN   OrderedLocusNames=Z3464, ECs3096;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Chaperone for NapA, the catalytic subunit of the periplasmic
CC       nitrate reductase. It binds directly and specifically to the twin-
CC       arginine signal peptide of NapA, preventing premature interaction with
CC       the Tat translocase and premature export. {ECO:0000255|HAMAP-
CC       Rule:MF_02200}.
CC   -!- SUBUNIT: Interacts with the cytoplasmic NapA precursor.
CC       {ECO:0000255|HAMAP-Rule:MF_02200}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02200,
CC       ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the NapD family. {ECO:0000255|HAMAP-
CC       Rule:MF_02200}.
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DR   EMBL; AE005174; AAG57342.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB36519.1; -; Genomic_DNA.
DR   PIR; B85860; B85860.
DR   PIR; H91015; H91015.
DR   RefSeq; NP_311123.1; NC_002695.1.
DR   RefSeq; WP_000557378.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0A9I6; -.
DR   BMRB; P0A9I6; -.
DR   SMR; P0A9I6; -.
DR   STRING; 155864.EDL933_3372; -.
DR   EnsemblBacteria; AAG57342; AAG57342; Z3464.
DR   EnsemblBacteria; BAB36519; BAB36519; ECs_3096.
DR   GeneID; 67416643; -.
DR   GeneID; 916802; -.
DR   KEGG; ece:Z3464; -.
DR   KEGG; ecs:ECs_3096; -.
DR   PATRIC; fig|386585.9.peg.3230; -.
DR   eggNOG; COG3062; Bacteria.
DR   HOGENOM; CLU_155794_1_0_6; -.
DR   OMA; ENQGFIT; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005048; F:signal sequence binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051224; P:negative regulation of protein transport; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_02200; NapD; 1.
DR   InterPro; IPR005623; Chaperone_NapD_NO3_reduct.
DR   PANTHER; PTHR38603; PTHR38603; 1.
DR   Pfam; PF03927; NapD; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Reference proteome.
FT   CHAIN           1..87
FT                   /note="Chaperone NapD"
FT                   /id="PRO_0000096712"
SQ   SEQUENCE   87 AA;  9469 MW;  EE59DF4EF17F650D CRC64;
     MHTNWQVCSL VVQAKSERIS DISTQLNAFP GCEVAVSDAP SGQLIVVVEA EDSETLIQTI
     ESVRNVEGVL AVSLVYHQQE EQGEETP
 
 
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