NLPI_ECOBW
ID NLPI_ECOBW Reviewed; 294 AA.
AC C4ZSQ4;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Lipoprotein NlpI;
DE Flags: Precursor;
GN Name=nlpI; OrderedLocusNames=BWG_2867;
OS Escherichia coli (strain K12 / MC4100 / BW2952).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=595496;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MC4100 / BW2952;
RX PubMed=19376874; DOI=10.1128/jb.00118-09;
RA Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA Wang L.;
RT "Genomic sequencing reveals regulatory mutations and recombinational events
RT in the widely used MC4100 lineage of Escherichia coli K-12.";
RL J. Bacteriol. 191:4025-4029(2009).
RN [2]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / BW2952;
RX PubMed=21705547; DOI=10.1128/aem.00648-11;
RA Charoenwong D., Andrews S., Mackey B.;
RT "The role of rpoS in the development of cell envelope resilience and
RT pressure resistance in stationary phase Escherichia coli.";
RL Appl. Environ. Microbiol. 77:5220-5229(2011).
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}.
CC -!- INDUCTION: By high-pressure. {ECO:0000269|PubMed:21705547}.
CC -!- DISRUPTION PHENOTYPE: Mutants were more sensitive to high pressure
CC treatment at of 300 MPa and failed to reseal the membrane after
CC treatment. {ECO:0000269|PubMed:21705547}.
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DR EMBL; CP001396; ACR62380.1; -; Genomic_DNA.
DR RefSeq; WP_000802080.1; NC_012759.1.
DR AlphaFoldDB; C4ZSQ4; -.
DR SMR; C4ZSQ4; -.
DR GeneID; 67414899; -.
DR KEGG; ebw:BWG_2867; -.
DR HOGENOM; CLU_071600_0_0_6; -.
DR OMA; VEHRYSF; -.
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 2: Evidence at transcript level;
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_0000413474"
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
