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Database: UniProt
Entry: A0A1N6MTF6_9GAMM
LinkDB: A0A1N6MTF6_9GAMM
Original site: A0A1N6MTF6_9GAMM 
ID   A0A1N6MTF6_9GAMM        Unreviewed;       350 AA.
AC   A0A1N6MTF6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Murein hydrolase activator NlpD {ECO:0000256|ARBA:ARBA00040670};
GN   Name=nlpD {ECO:0000313|EMBL:SIP72116.1};
GN   ORFNames=XIS1_1350021 {ECO:0000313|EMBL:SIP72116.1};
OS   Xenorhabdus innexi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=290109 {ECO:0000313|EMBL:SIP72116.1, ECO:0000313|Proteomes:UP000196435};
RN   [1] {ECO:0000313|Proteomes:UP000196435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HGB1681 (deposited as PTA-6826 in the American Type Culture
RC   Collection) {ECO:0000313|Proteomes:UP000196435};
RA   Gaudriault S.;
RL   Submitted (DEC-2016) 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. {ECO:0000256|ARBA:ARBA00037728}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004519}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004519}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004635}.
CC   -!- SIMILARITY: Belongs to the E.coli NlpD/Haemophilus LppB family.
CC       {ECO:0000256|ARBA:ARBA00038420}.
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DR   EMBL; FTLG01000041; SIP72116.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1N6MTF6; -.
DR   OrthoDB; 9795421at2; -.
DR   Proteomes; UP000196435; Unassembled WGS sequence.
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:SF290; 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 inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000313|EMBL:SIP72116.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196435}.
FT   DOMAIN          113..157
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   REGION          49..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   350 AA;  38246 MW;  30DC46FE09A2CD86 CRC64;
     MKVGNLMKKI QWIIIYTIAG TILAGCSNTP NHPAPIVSVD NQEKNRIISS RPSSVSTPMP
     SSPPVISKNR ATDNNASNSR YLDNRAGGNS LQQGRIVYNR NYGNIPKGSY NGKTYTVKHG
     DTLFYIAWIT GKDFRELSHI NSISEPYGLN VGQVLRIGNV NSINGVSVAS NSTQSKIEQV
     DFQKSNAYPA NIDRHNSQKT LPRETISGSD DAPYKASSAA DLNASRPINN WRWPAEGKIL
     EGFSDSQGGN KGIDIAGNRG QPVFATASGK VVYAGNALRG YGNLIIIKHD DDYLSAYAHN
     DTMLVREQQD VQAGQKIATM GSTGTSSVRL HFEIRYKGKS VNPLRYLPQR
//
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