NLPD_SALTY
ID NLPD_SALTY Reviewed; 377 AA.
AC P40827;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Murein hydrolase activator NlpD;
DE Flags: Precursor;
GN Name=nlpD; OrderedLocusNames=STM2925;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 280-377.
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=8086465; DOI=10.1016/0167-4781(94)90271-2;
RA Prince R.W., Fang F.C., Libby S.J.;
RT "Cloning and sequencing of the gene encoding the RpoS (KatF) sigma factor
RT from Salmonella typhimurium 14028s.";
RL Biochim. Biophys. Acta 1219:198-200(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 298-377.
RC STRAIN=C52;
RX PubMed=7961444; DOI=10.1128/jb.176.22.6852-6860.1994;
RA Kowarz L., Coynault C., Robbe-Saule V., Norel F.;
RT "The Salmonella typhimurium katF (rpoS) gene: cloning, nucleotide sequence,
RT and regulation of spvR and spvABCD virulence plasmid genes.";
RL J. Bacteriol. 176:6852-6860(1994).
CC -!- FUNCTION: Activator of the cell wall hydrolase AmiC. Required for
CC septal murein cleavage and daughter cell separation during cell
CC division (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303}. Note=Localizes at the septal
CC ring. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the E.coli NlpD/Haemophilus LppB family.
CC {ECO:0000305}.
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DR EMBL; AE006468; AAL21805.1; -; Genomic_DNA.
DR EMBL; U05011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X77752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S58445; S58445.
DR RefSeq; NP_461846.1; NC_003197.2.
DR RefSeq; WP_001272632.1; NC_003197.2.
DR AlphaFoldDB; P40827; -.
DR SMR; P40827; -.
DR STRING; 99287.STM2925; -.
DR PaxDb; P40827; -.
DR EnsemblBacteria; AAL21805; AAL21805; STM2925.
DR GeneID; 1254448; -.
DR KEGG; stm:STM2925; -.
DR PATRIC; fig|99287.12.peg.3079; -.
DR HOGENOM; CLU_029425_0_1_6; -.
DR OMA; TMFLIAY; -.
DR PhylomeDB; P40827; -.
DR BioCyc; SENT99287:STM2925-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0009279; C:cell outer membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IBA:GO_Central.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 2.70.70.10; -; 1.
DR Gene3D; 3.10.350.10; -; 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR016047; Peptidase_M23.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF01551; Peptidase_M23; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF51261; SSF51261; 1.
DR PROSITE; PS51782; LYSM; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Repeat; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 26..377
FT /note="Murein hydrolase activator NlpD"
FT /id="PRO_0000018032"
FT DOMAIN 119..163
FT /note="LysM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT REPEAT 203..209
FT /note="1"
FT REPEAT 225..231
FT /note="2"
FT REPEAT 237..243
FT /note="3"
FT REPEAT 244..250
FT /note="4"
FT REGION 30..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..250
FT /note="4 X 7 AA approximate repeats"
FT LIPID 26
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 26
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CONFLICT 377
FT /note="R -> P (in Ref. 2; U05011)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 39641 MW; 27C29D77A145ABF0 CRC64;
MSAGSPKFTV SRIAALSLVS LWLAGCTSSS NPPAPVTSVD SGSSSNTNSG MLITPPPKMG
ATTQQTPQQA PQIQPVQRPV TQPMQTQPVT EQPVQMENGR IVYNRQYGNI PKGSYTGGST
YTVKKGDTLF YIAWITGNDF RDLAQRNSIS APYSLNVGQT LQVGNASGTP ITGGNAITQA
DAAQQGVVTR SAQNSTVAVA SQPTITYSEG SGEQSANKML PNNKPAGTVV TAPVTAPTVS
TTEPNASSTS TSAPISAWRW PTDGKVIENF GASEGGNKGI DIAGSKGQAI VATADGRVVY
AGNALRGYGN LIIIKHNDDY LSAYAHNDTM LVREQQEVKA GQKIATMGST GTSSTRLHFE
IRYKGKSVNP LRYLPQR
