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NLPI_YERPN
ID   NLPI_YERPN              Reviewed;         294 AA.
AC   Q1CM50;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Lipoprotein NlpI;
DE   Flags: Precursor;
GN   Name=nlpI; OrderedLocusNames=YPN_0598; ORFNames=YP516_0629;
OS   Yersinia pestis bv. Antiqua (strain Nepal516).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=377628;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RA   Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA   Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA   Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT   "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in cell division. May play a role in
CC       bacterial septation or regulation of cell wall degradation during cell
CC       division (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
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DR   EMBL; CP000305; ABG16930.1; -; Genomic_DNA.
DR   EMBL; ACNQ01000006; EEO78392.1; -; Genomic_DNA.
DR   RefSeq; WP_002209260.1; NZ_ACNQ01000006.1.
DR   AlphaFoldDB; Q1CM50; -.
DR   SMR; Q1CM50; -.
DR   EnsemblBacteria; ABG16930; ABG16930; YPN_0598.
DR   GeneID; 66843096; -.
DR   KEGG; ypn:YPN_0598; -.
DR   HOGENOM; CLU_071600_0_0_6; -.
DR   OMA; VEHRYSF; -.
DR   Proteomes; UP000008936; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR023605; Lipoprotein_NlpI.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR013105; TPR_2.
DR   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF07719; TPR_2; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   PIRSF; PIRSF004654; NlpI; 1.
DR   SMART; SM00028; TPR; 2.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS50005; TPR; 4.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW   Repeat; Signal; TPR repeat.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           19..294
FT                   /note="Lipoprotein NlpI"
FT                   /id="PRO_0000413486"
FT   REPEAT          62..95
FT                   /note="TPR 1"
FT   REPEAT          96..129
FT                   /note="TPR 2"
FT   REPEAT          234..267
FT                   /note="TPR 3"
FT   LIPID           19
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           19
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   294 AA;  33741 MW;  E12D53FBDF79B2A0 CRC64;
     MKPFLRWCYV ATALMLAGCS NHDWRKDEVL AIPLQPTLQQ EVILARMEQI LASRALTDDE
     RAQLLYERGV LYDSLGLRAL ARNDFSQALA IRPDMPEVFN YLGIYLTQAG NFDAAYEAFD
     SVLELDPTYN YARLNRGIAL YYGGRFPLAQ DDLQAFYQDD PNDPFRSLWL YLVEREIDPK
     AAVVALQQRY EKSDRGQWGW NIVEFYLGKI SEKSLMERLK ADATDNTSLA EHLSETDFYL
     GKHYLSLGDK NTASVLFKLT VANNVHNFVE HRYALLELAL LGQEQDDLSE SDQQ
 
 
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