ID E6WG91_PANSA Unreviewed; 362 AA.
AC E6WG91;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Murein hydrolase activator NlpD {ECO:0000256|ARBA:ARBA00040670};
DE Flags: Precursor;
GN OrderedLocusNames=Pat9b_3072 {ECO:0000313|EMBL:ADU70371.1};
OS Pantoea sp. (strain At-9b).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=592316 {ECO:0000313|EMBL:ADU70371.1, ECO:0000313|Proteomes:UP000001624};
RN [1] {ECO:0000313|EMBL:ADU70371.1, ECO:0000313|Proteomes:UP000001624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=At-9b {ECO:0000313|EMBL:ADU70371.1,
RC ECO:0000313|Proteomes:UP000001624};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pinto A., Currie C., Woyke T.;
RT "Complete sequence chromosome of Pantoea sp. At-9b.";
RL Submitted (DEC-2010) 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; CP002433; ADU70371.1; -; Genomic_DNA.
DR RefSeq; WP_013510223.1; NC_014837.1.
DR AlphaFoldDB; E6WG91; -.
DR STRING; 592316.Pat9b_3072; -.
DR KEGG; pao:Pat9b_3072; -.
DR eggNOG; COG1388; Bacteria.
DR eggNOG; COG4942; Bacteria.
DR HOGENOM; CLU_029425_0_1_6; -.
DR OrthoDB; 9795421at2; -.
DR Proteomes; UP000001624; 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.
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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..362
FT /note="Murein hydrolase activator NlpD"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003214658"
FT DOMAIN 106..150
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 194..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 362 AA; 37437 MW; 43169909CC060828 CRC64;
MSTGSTTFQL RRLAALTLVG FWLAGCSSSD NTQAPISQIG GNGGMSDSSG GGVPTMPHGG
MLSGGVPSAP PSGGMISGNN NVTTENGRIV YNRNYGNIPK GSYGGETYTV KRGDTLFYIA
WITGNDYRDL AQRNNIPAPY SLNAGQTLQV GNGAGQSITG GNAITVADAT QGGVPATPGS
SQIKSAPVAQ QPVITYSDDS GNSSGSKLLP SKGANNVATT TAPVTVPPTV SSTTDSTTPV
GSWRWPTDGK IIDNFSAAEG GNKGIDIAGS RGQPVVATAS GRVVYAGNAL RGYGNLIIIK
HNDDYLSAYA HNDTMLVREQ QEVKAGQKIA TMGSTGTSSV RLHFEIRYKG KSVNPLRYLP
QR
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