NLPI_ECOLU
ID NLPI_ECOLU Reviewed; 294 AA.
AC B7NDE9;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Lipoprotein NlpI;
DE Flags: Precursor;
GN Name=nlpI; OrderedLocusNames=ECUMN_3645;
OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN026 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928163; CAR14799.1; -; Genomic_DNA.
DR RefSeq; WP_000802087.1; NC_011751.1.
DR RefSeq; YP_002414304.1; NC_011751.1.
DR AlphaFoldDB; B7NDE9; -.
DR SMR; B7NDE9; -.
DR STRING; 585056.ECUMN_3645; -.
DR EnsemblBacteria; CAR14799; CAR14799; ECUMN_3645.
DR KEGG; eum:ECUMN_3645; -.
DR PATRIC; fig|585056.7.peg.3825; -.
DR HOGENOM; CLU_071600_0_0_6; -.
DR OMA; VEHRYSF; -.
DR Proteomes; UP000007097; 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_0000413475"
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; 33649 MW; D7D84AADF65A01DB CRC64;
MKPFLRWCFV ATALTLAGCS NTSWRKSEVL AVPLQPTLQQ EVILARMEQI LASRALTDDE
RAQLLYERGV LYDSLGLRAL ARNDFSQALA IRPDMPEVFN YLGIYLTQAG NFDAAYEAFD
SVLELDPTYN YAHLNRGIAL YYGGRDKLAQ DDLLAFYQDD PNDPFRSLWL YLAEQKLDEK
QAKEVLRQHF EKSDKEQWGW NIVEFYLGNI SEQTLMERLK ADATDNTSLA EHLSETNFYL
GKYYLSLGDL DSATALFKLA VANNVHNFVE HRYALLELSL LGQDQDDLAE SDQQ
