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Database: UniProt
Entry: NLPD_SHIFL
LinkDB: NLPD_SHIFL
Original site: NLPD_SHIFL 
ID   NLPD_SHIFL              Reviewed;         379 AA.
AC   P0ADA4; P33648;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   24-JAN-2024, entry version 123.
DE   RecName: Full=Murein hydrolase activator NlpD;
DE   Flags: Precursor;
GN   Name=nlpD; OrderedLocusNames=SF2765, S2958;
OS   Shigella flexneri.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN44254.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP18080.1; -; Genomic_DNA.
DR   RefSeq; NP_708547.2; NC_004337.2.
DR   RefSeq; WP_001272592.1; NZ_WPGW01000039.1.
DR   AlphaFoldDB; P0ADA4; -.
DR   SMR; P0ADA4; -.
DR   STRING; 198214.SF2765; -.
DR   PaxDb; 198214-SF2765; -.
DR   GeneID; 1025716; -.
DR   GeneID; 75172823; -.
DR   KEGG; sfl:SF2765; -.
DR   KEGG; sfx:S2958; -.
DR   PATRIC; fig|198214.7.peg.3291; -.
DR   HOGENOM; CLU_029425_0_1_6; -.
DR   OMA; KGDTMFL; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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   CDD; cd00118; LysM; 1.
DR   CDD; cd12797; M23_peptidase; 1.
DR   Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR   Gene3D; 3.10.350.10; LysM domain; 1.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR016047; Peptidase_M23.
DR   PANTHER; PTHR21666:SF263; MUREIN HYDROLASE ACTIVATOR NLPD; 1.
DR   PANTHER; PTHR21666; PEPTIDASE-RELATED; 1.
DR   Pfam; PF01476; LysM; 1.
DR   Pfam; PF01551; Peptidase_M23; 1.
DR   SMART; SM00257; LysM; 1.
DR   SUPFAM; SSF51261; Duplicated hybrid motif; 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..379
FT                   /note="Murein hydrolase activator NlpD"
FT                   /id="PRO_0000043183"
FT   REPEAT          66..73
FT                   /note="1-1"
FT   REPEAT          74..81
FT                   /note="1-2; approximate"
FT   REPEAT          82..89
FT                   /note="1-3"
FT   REPEAT          90..97
FT                   /note="1-4; approximate"
FT   DOMAIN          121..165
FT                   /note="LysM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   REPEAT          205..211
FT                   /note="2-1"
FT   REPEAT          227..233
FT                   /note="2-2"
FT   REPEAT          239..245
FT                   /note="2-3"
FT   REPEAT          246..252
FT                   /note="2-4"
FT   REGION          30..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          66..97
FT                   /note="4 X 8 AA tandem repeats of Q-Q-P-Q-I-Q-P-V"
FT   REGION          205..252
FT                   /note="4 X 7 AA approximate repeats"
FT   REGION          210..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          240..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   379 AA;  40149 MW;  A8E6A2B8456105FE CRC64;
     MSAGSPKFTV RRIAALSLVS LWLAGCSDTS NPPAPVSSVN GNAPANTNSG MLITPPPKMG
     TTSTAQQPQI QPVQQPQIQA TQQPQIQPVQ PVAQQPVQME NGRIVYNRQY GNIPKGSYSG
     STYTVKKGDT LFYIAWITGN DFRDLAQRNN IQAPYALNVG QTLQVGNASG TPITGGNAIT
     QADAAEQGVV IKPAQNSTVA VASQPTITYS ESSGEQSANK MLPNNKPTAT TVTAPVTVPT
     ASTTEPTVSS TSTSTPISTW RWPTEGKVIE TFGASEGGNK GIDIAGSKGQ AIIATADGRV
     VYAGNALRGY GNLIIIKHND DYLSAYAHND TMLVREQQEV KAGQKIATMG STGTSSTRLH
     FEIRYKGKSV NPLRYLPQR
//
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