ID A0A177H5L3_9RHOB Unreviewed; 374 AA.
AC A0A177H5L3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Murein hydrolase activator NlpD {ECO:0000313|EMBL:OAH06236.1};
GN Name=nlpD {ECO:0000313|EMBL:OAH06236.1};
GN ORFNames=pfor_33c2998 {ECO:0000313|EMBL:OAH06236.1};
OS Rhodobacteraceae bacterium SB2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1689867 {ECO:0000313|EMBL:OAH06236.1, ECO:0000313|Proteomes:UP000077333};
RN [1] {ECO:0000313|EMBL:OAH06236.1, ECO:0000313|Proteomes:UP000077333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB2 {ECO:0000313|EMBL:OAH06236.1,
RC ECO:0000313|Proteomes:UP000077333};
RA Poehlein A., Billerbeck S., Voget S., Wemheuer B., Giebel H.-A.,
RA Brinkhoff T., Daniel R., Simon M.;
RT "A new prominent pelagic Roseobacter clade subcluster - CHAB-I-5:
RT biogeography and genomic comparison to other roseobacters.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAH06236.1}.
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DR EMBL; LGRT01000034; OAH06236.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177H5L3; -.
DR STRING; 1689867.pfor_33c2998; -.
DR PATRIC; fig|1689867.3.peg.2964; -.
DR OrthoDB; 9795421at2; -.
DR Proteomes; UP000077333; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 2.
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; 2.
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:SF270; OUTER MEMBRANE ANTIGENIC LIPOPROTEIN B; 1.
DR PANTHER; PTHR21666; PEPTIDASE-RELATED; 1.
DR Pfam; PF01476; LysM; 2.
DR Pfam; PF01551; Peptidase_M23; 1.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR PROSITE; PS51782; LYSM; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:OAH06236.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077333};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..374
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008062546"
FT DOMAIN 64..108
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 154..198
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 135..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 374 AA; 39911 MW; F05088A3DD068F8B CRC64;
MFRPTAVSFS LSCLSAIILA GCDTSGFDLD MRQNQYDTSA AAQRVATPRA EPDDLGIIEY
PTYQVVVARE GDTVTSIANR LGLTPNSLAS YNGVSREKTM RVGEVLALPK FSENAATQSA
EIDVSALTQS ALAKVETSQA STTSQPATNK DEPIRHKVRR GETAFTISRL YNVSIRSLSE
WNGLDSNFTI REDQYLLIPL TLEVPITAPK TRPEKPGQGS QTPVPPSSST PLPKAESATA
SQVTPLKEKA PVQEAVATTG KLTYPVNGKI IREYVKGKTE GIDLSAPAGS TIVAAETGTV
AAITADVDQV PIVVIKHANE LLTVYANVGN ISVSKGAKVS RGQAIGKIPP SNPTYLHFEV
RQGLDSVDPL DYLQ
//
