NLPD_SALDU
ID NLPD_SALDU Reviewed; 377 AA.
AC P39700;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Murein hydrolase activator NlpD;
DE Flags: Precursor;
GN Name=nlpD;
OS Salmonella dublin.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=98360;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=Lane;
RX PubMed=9973354; DOI=10.1128/jb.181.4.1264-1268.1999;
RA Paesold G., Krause M.;
RT "Analysis of rpoS mRNA in Salmonella dublin: identification of multiple
RT transcripts with growth-phase dependent variation in transcript
RT stability.";
RL J. Bacteriol. 181:1264-1268(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 284-377.
RC STRAIN=Lane;
RA Krause M.W., El-Gedaily A.;
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
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; AJ006131; CAA06881.1; -; Genomic_DNA.
DR EMBL; X82129; CAA57639.1; -; Genomic_DNA.
DR PIR; S49470; S49470.
DR RefSeq; WP_001272631.1; NZ_VDCP01000001.1.
DR AlphaFoldDB; P39700; -.
DR SMR; P39700; -.
DR PATRIC; fig|98360.39.peg.2646; -.
DR OMA; TMFLIAY; -.
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 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 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; Lipoprotein;
KW Membrane; Palmitate; 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_0000018030"
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"
SQ SEQUENCE 377 AA; 39671 MW; DC7F59B943F86512 CRC64;
MSAGSPKFTV SRIAALSLVS LWLAGCTSSS NPPAPVTSVD SGSSSNTNSG MLITPPPKMG
ATTQQTPQQA PQIQPVQRPV TQPMQTQPVT EQPVQMENGR IVYNRQYGNI PKGSYTGGST
YTVKKGDTLF YIAWITGNDF RDLAQRNSIS APYSLNVGQT LQVGNASGMP ITGGNAITQA
DAAQQGVVTR SAQNSTVAVA SQPTITYSEG SGEQSANKML PNNKPAGTVV TAPVTAPTVS
TTEPNASSTS TSAPISAWRW PTDGKVIENF GASEGGNKGI DIAGSKGQAI VATADGRVVY
AGNALRGYGN LIIIKHNDDY LSAYAHNDTM LVREQQEVKA GQKIATMGST GTSSTRLHFE
IRYKGKSVNP LRYLPQR