ID   PGRP1_HOLDI             Reviewed;         197 AA.
AC   Q765P4;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Peptidoglycan-recognition protein 1;
DE   AltName: Full=Hd-PGRP-1;
DE   Flags: Precursor;
GN   Name=PGRP-1;
OS   Holotrichia diomphalia (Korean black chafer).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC   Scarabaeidae; Melolonthinae; Holotrichia.
OX   NCBI_TaxID=33394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-38, FUNCTION,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Larva;
RX   PubMed=14583608; DOI=10.1074/jbc.m309821200;
RA   Lee M.H., Osaki T., Lee J.Y., Baek M.J., Zhang R., Park J.W., Kawabata S.,
RA   Soederhaell K., Lee B.L.;
RT   "Peptidoglycan recognition proteins involved in 1,3-beta-D-glucan-dependent
RT   prophenoloxidase activation system of insect.";
RL   J. Biol. Chem. 279:3218-3227(2004).
CC   -!- FUNCTION: Peptidoglycan-recognition protein probably involved in innate
CC       immunity by binding to peptidoglycans (PGN) of bacteria and activating
CC       the prophenoloxidase (proPO) cascade immune response. Binds to 1,3-
CC       beta-D-glucan and PGN. {ECO:0000269|PubMed:14583608}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14583608}.
CC   -!- TISSUE SPECIFICITY: Localizes to plasma (at protein level).
CC       {ECO:0000269|PubMed:14583608}.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AB115774; BAD08316.1; -; mRNA.
DR   AlphaFoldDB; Q765P4; -.
DR   SMR; Q765P4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; -; 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; PTHR11022; 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; SSF55846; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Immunity; Innate immunity;
KW   Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:14583608"
FT   CHAIN           24..197
FT                   /note="Peptidoglycan-recognition protein 1"
FT                   /id="PRO_0000023916"
FT   DOMAIN          53..180
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..154
FT                   /evidence="ECO:0000250"
FT   DISULFID        68..74
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   197 AA;  22092 MW;  2F6345018D9B7F84 CRC64;
     MKLATITFFL LTEIFFYISY AEATRSGPDL CPTIISKRDW GGNAALRVGY TSKPLERVVI
     HHTVTPECAN EARCSSRMVS MQNYHMDELG YDDISYNFVI GGDGRVYEGV GWHKKGSHSP
     GWDSQSIGIA FIGDFTNKLP SREMLDAAKD LIVCAIELGE LTRGYKLLGA RNVKATKSPG
     DKLYREIQNW EGFTRRP