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
