ID A0A0T6B3C0_9SCAR Unreviewed; 210 AA.
AC A0A0T6B3C0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Peptidoglycan-recognition protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=AMK59_5022 {ECO:0000313|EMBL:KRT81351.1};
OS Oryctes borbonicus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC Scarabaeidae; Dynastinae; Oryctes.
OX NCBI_TaxID=1629725 {ECO:0000313|EMBL:KRT81351.1, ECO:0000313|Proteomes:UP000051574};
RN [1] {ECO:0000313|EMBL:KRT81351.1, ECO:0000313|Proteomes:UP000051574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OB123 {ECO:0000313|EMBL:KRT81351.1};
RC TISSUE=Whole animal {ECO:0000313|EMBL:KRT81351.1};
RA Meyer J.M., Markov G.V., Baskaran P., Herrmann M., Sommer R.J.,
RA Roedelsperger C.;
RT "Draft genome of the scarab beetle Oryctes borbonicus.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000256|ARBA:ARBA00007553}.
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:KRT81351.1}.
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DR EMBL; LJIG01016188; KRT81351.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6B3C0; -.
DR OrthoDB; 2282228at2759; -.
DR Proteomes; UP000051574; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd06583; PGRP; 1.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR017331; Peptidoglycan_recognition.
DR InterPro; IPR015510; PGRP.
DR InterPro; IPR006619; PGRP_domain_met/bac.
DR PANTHER; PTHR11022; PEPTIDOGLYCAN RECOGNITION PROTEIN; 1.
DR PANTHER; PTHR11022:SF79; PEPTIDOGLYCAN RECOGNITION PROTEIN 5; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR PIRSF; PIRSF037945; PGRPs; 1.
DR SMART; SM00644; Ami_2; 1.
DR SMART; SM00701; PGRP; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR037945-1}; Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Reference proteome {ECO:0000313|Proteomes:UP000051574};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..210
FT /note="Peptidoglycan-recognition protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006668322"
FT DOMAIN 45..187
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT DOMAIN 56..193
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT DISULFID 44..167
FT /evidence="ECO:0000256|PIRSR:PIRSR037945-1"
FT DISULFID 81..87
FT /evidence="ECO:0000256|PIRSR:PIRSR037945-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRT81351.1"
SQ SEQUENCE 210 AA; 23210 MW; 193FF3F47ED75138 CRC64;
FMLQNLSWHY TPVTYASKMT RALCLLLLLC TEISLIFAKL PDVCPPIISK SQWGGRDSAK
VQHIIIPLKY AIIHHTATPG CSDQAACSQK IVNMQSYHMD KLGFDDIGYN FLIGGDGNVY
AGAGWHRQGA HTRGYNTKSI GIGFIGDYSS TPPSSKQIEA AKKLIECGVA LKELDERYKL
LGARSVRPTE SPGTALYREI QNWRGFTTTP
//
