ID B1LFR5_ECOSM Unreviewed; 294 AA.
AC B1LFR5;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Lipoprotein NlpI {ECO:0000256|ARBA:ARBA00018294, ECO:0000256|PIRNR:PIRNR004654};
GN Name=nlpI {ECO:0000313|EMBL:ACB18531.1};
GN OrderedLocusNames=EcSMS35_3459 {ECO:0000313|EMBL:ACB18531.1};
OS Escherichia coli (strain SMS-3-5 / SECEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=439855 {ECO:0000313|EMBL:ACB18531.1, ECO:0000313|Proteomes:UP000007011};
RN [1] {ECO:0000313|EMBL:ACB18531.1, ECO:0000313|Proteomes:UP000007011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS-3-5 / SECEC {ECO:0000313|Proteomes:UP000007011};
RX PubMed=18708504; DOI=10.1128/JB.00661-08;
RA Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA Ravel J., Stepanauskas R.;
RT "Insights into the environmental resistance gene pool from the genome
RT sequence of the multidrug-resistant environmental isolate Escherichia coli
RT SMS-3-5.";
RL J. Bacteriol. 190:6779-6794(2008).
CC -!- FUNCTION: May be involved in cell division.
CC {ECO:0000256|PIRNR:PIRNR004654}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR004654}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR004654}.
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DR EMBL; CP000970; ACB18531.1; -; Genomic_DNA.
DR RefSeq; WP_000802080.1; NC_010498.1.
DR AlphaFoldDB; B1LFR5; -.
DR SMR; B1LFR5; -.
DR GeneID; 83579304; -.
DR KEGG; ecm:EcSMS35_3459; -.
DR HOGENOM; CLU_071600_0_0_6; -.
DR Proteomes; UP000007011; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR023605; Lipoprotein_NlpI.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR44858; TETRATRICOPEPTIDE REPEAT PROTEIN 6; 1.
DR PANTHER; PTHR44858:SF1; UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE SPINDLY-RELATED; 1.
DR Pfam; PF13432; TPR_16; 1.
DR PIRSF; PIRSF004654; NlpI; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50005; TPR; 3.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR004654}; Lipoprotein {ECO:0000313|EMBL:ACB18531.1};
KW Membrane {ECO:0000256|PIRNR:PIRNR004654};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}.
FT REPEAT 62..95
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 96..129
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 234..267
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
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
//
