ID   NLPI_ECOK1              Reviewed;         294 AA.
AC   A1AG68;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Lipoprotein NlpI;
DE   Flags: Precursor;
GN   Name=nlpI; OrderedLocusNames=Ecok1_31640; ORFNames=APECO1_3267;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
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; CP000468; ABJ02658.1; -; Genomic_DNA.
DR   RefSeq; WP_000802080.1; NC_008563.1.
DR   AlphaFoldDB; A1AG68; -.
DR   SMR; A1AG68; -.
DR   EnsemblBacteria; ABJ02658; ABJ02658; APECO1_3267.
DR   GeneID; 67414899; -.
DR   KEGG; ecv:APECO1_3267; -.
DR   HOGENOM; CLU_071600_0_0_6; -.
DR   OMA; VEHRYSF; -.
DR   Proteomes; UP000008216; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 3.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 2.
PE   3: Inferred from homology;
KW   Cell membrane; Lipoprotein; Membrane; Palmitate; Repeat; Signal;
KW   TPR repeat.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           19..294
FT                   /note="Lipoprotein NlpI"
FT                   /id="PRO_0000413477"
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;  33621 MW;  4CA6724327A9CEE7 CRC64;
     MKPFLRWCFV ATALTLAGCS NTSWRKSEVL AVPLQPTLQQ EVILARMEQI LASRALTDDE
     RAQLLYERGV LYDSLGLRAL ARNDFSQALA IRPDMPEVFN YLGIYLTQAG NFDAAYEAFD
     SVLELDPTYN YAHLNRGIAL YYGGRDKLAQ DDLLAFYQDD PNDPFRSLWL YLAEQKLDEK
     QAKEVLKQHF EKSDKEQWGW NIVEFYLGNI SEQTLMERLK ADATDNTSLA EHLSETNFYL
     GKYYLSLGDL DSATALFKLA VANNVHNFVE HRYALLELSL LGQDQDDLAE SDQQ