ID Q2NVM0_SODGM Unreviewed; 362 AA.
AC Q2NVM0;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Murein hydrolase activator NlpD {ECO:0000256|ARBA:ARBA00040670};
GN OrderedLocusNames=SG0530 {ECO:0000313|EMBL:BAE73805.1};
OS Sodalis glossinidius (strain morsitans).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=343509 {ECO:0000313|EMBL:BAE73805.1, ECO:0000313|Proteomes:UP000001932};
RN [1] {ECO:0000313|EMBL:BAE73805.1, ECO:0000313|Proteomes:UP000001932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=morsitans {ECO:0000313|Proteomes:UP000001932};
RX PubMed=16365377; DOI=10.1101/gr.4106106;
RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA Aksoy S.;
RT "Massive genome erosion and functional adaptations provide insights into
RT the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL Genome Res. 16:149-156(2006).
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; AP008232; BAE73805.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2NVM0; -.
DR STRING; 343509.SG0530; -.
DR KEGG; sgl:SG0530; -.
DR eggNOG; COG1388; Bacteria.
DR eggNOG; COG4942; Bacteria.
DR HOGENOM; CLU_029425_0_1_6; -.
DR Proteomes; UP000001932; Chromosome.
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:BAE73805.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..362
FT /note="Murein hydrolase activator NlpD"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004213299"
FT DOMAIN 92..136
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 175..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 362 AA; 37991 MW; B0ED430BEDDC0D07 CRC64;
MSMGSPKSAW RRVAVCAMAS IWLAGCANNE SSAPISSVGG GSATTVERAP QLGQPRAVVS
GGEQGQVNVS PQGNIVYNRS YDNIQKGSYS GATYQVKRGD TLFYIAWITG NDYRDLAQRN
NIPEPYSLNV GQTLQVGNGT VPITGNAPAG TVLASNANQT NTGVVVALVP TSNTRLTESS
VDSNKNNGYP ESSSKQSVGK MLPSSNGKML PTTGTVVTTT APVAAPSTAP AATASGSTAI
TGWRWPTDGK IIDNFSAAEG GNKGVDISGS RGQPILATVS GRVVYAGNAL RGYGNLIIIK
HNDDYLSAYA HNDTMLVREQ QEVRAGQKIA TMGSTGTSTT RLHFEIRYKG KSVNPLRYLP
QR
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