NLPI_ECOL6
ID NLPI_ECOL6 Reviewed; 294 AA.
AC P0AFB2; P39833;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Lipoprotein NlpI;
DE Flags: Precursor;
GN Name=nlpI; OrderedLocusNames=c3918;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN82359.1; -; Genomic_DNA.
DR RefSeq; WP_000802080.1; NC_004431.1.
DR AlphaFoldDB; P0AFB2; -.
DR SMR; P0AFB2; -.
DR STRING; 199310.c3918; -.
DR EnsemblBacteria; AAN82359; AAN82359; c3918.
DR GeneID; 67414899; -.
DR KEGG; ecc:c3918; -.
DR eggNOG; COG4785; Bacteria.
DR HOGENOM; CLU_071600_0_0_6; -.
DR OMA; VEHRYSF; -.
DR BioCyc; ECOL199310:C3918-MON; -.
DR Proteomes; UP000001410; 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_0000045128"
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
