ID   NLPI_ECOL5              Reviewed;         294 AA.
AC   Q0TCU6;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Lipoprotein NlpI;
DE   Flags: Precursor;
GN   Name=nlpI; OrderedLocusNames=ECP_3251;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
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; CP000247; ABG71233.1; -; Genomic_DNA.
DR   RefSeq; WP_000802080.1; NC_008253.1.
DR   AlphaFoldDB; Q0TCU6; -.
DR   SMR; Q0TCU6; -.
DR   STRING; 362663.ECP_3251; -.
DR   EnsemblBacteria; ABG71233; ABG71233; ECP_3251.
DR   GeneID; 67414899; -.
DR   KEGG; ecp:ECP_3251; -.
DR   HOGENOM; CLU_071600_0_0_6; -.
DR   OMA; VEHRYSF; -.
DR   Proteomes; UP000009182; 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; 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 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_0000413478"
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