ID Q6D1B7_PECAS Unreviewed; 344 AA.
AC Q6D1B7;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Murein hydrolase activator NlpD {ECO:0000256|ARBA:ARBA00040670};
GN Name=nlpD {ECO:0000313|EMBL:CAG76429.1};
GN OrderedLocusNames=ECA3531 {ECO:0000313|EMBL:CAG76429.1};
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491 {ECO:0000313|EMBL:CAG76429.1, ECO:0000313|Proteomes:UP000007966};
RN [1] {ECO:0000313|EMBL:CAG76429.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SCRI1043 {ECO:0000313|EMBL:CAG76429.1};
RA Bell K.S., Sebaihia M., Pritchard L., Holden M., Hyman L.J., Holeva M.C.,
RA Thomson N.R., Bentley S.D., Churcher C., Mungall K., Atkin R., Bason N.,
RA Brooks K., Chillingworth T., Clark K., Doggett J., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Norbertczak H., Ormond D., Price C.,
RA Quail M.A., Sanders M., Walker D., Whitehead S., Salmond G.P.C.,
RA Birch P.R.J., Barrell B.G., Parkhill J., Toth I.K.;
RT "The genome sequence of the enterobacterial phytopathogen Erwinia
RT carotovora subsp. atroseptica SCRI1043 and functional genomic
RT identification of novel virulence factors.";
RL Submitted (FEB-2004) 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; BX950851; CAG76429.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6D1B7; -.
DR STRING; 218491.ECA3531; -.
DR KEGG; eca:ECA3531; -.
DR eggNOG; COG1388; Bacteria.
DR eggNOG; COG4942; Bacteria.
DR HOGENOM; CLU_029425_0_1_6; -.
DR OrthoDB; 9795421at2; -.
DR Proteomes; UP000007966; 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:CAG76429.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000007966}.
FT DOMAIN 88..132
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 32..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 344 AA; 35618 MW; 64078B4E3856C1F9 CRC64;
MGSRMMNLRH IAACMVIVLG VAGCSNNNSK SAPISSVDGN TGSRGGMLSA PPSRISTAGE
SVAATSEGRI VYNRSYGNIP KGSYSGGNAY TVKRGDTLFY IAWITGNDYR DLAQRNNIPE
PYSLNVGQSL SLGSGSGNNA SGGGMMSGGG MLATTDATRG GVPTPPSSAQ IQTTSVDSQS
TNAYSGNQGK QNVGKMLPTA GATTTAPVSA PAAVASSNTA AVSSWRWPTD GKVIDSFSDS
EGGNKGIDIA GSRGQPITAT ANGRVVYAGN ALRGYGNLII IKHNDDYLSA YAHNDTMLVR
EQQDVTAGQK IATMGSTGTS SVRLHFEIRY KGKSVNPLRF LPQR
//
