PGRP_BOMMO
ID PGRP_BOMMO Reviewed; 196 AA.
AC Q9XTN0; Q9TWD4;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Peptidoglycan recognition protein;
DE Flags: Precursor;
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 24-72;
RP 99-118; 147-159 AND 183-196, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=Kinshu X Showa; TISSUE=Fat body;
RX PubMed=10207004; DOI=10.1074/jbc.274.17.11854;
RA Ochiai M., Ashida M.;
RT "A pattern recognition protein for peptidoglycan. Cloning the cDNA and the
RT gene of the silkworm, Bombyx mori.";
RL J. Biol. Chem. 274:11854-11858(1999).
RN [2]
RP PROTEIN SEQUENCE OF 24-43, FUNCTION, AND SUBUNIT.
RC TISSUE=Hemolymph;
RX PubMed=8662762; DOI=10.1074/jbc.271.23.13854;
RA Yoshida H., Kinoshita K., Ashida M.;
RT "Purification of a peptidoglycan recognition protein from hemolymph of the
RT silkworm, Bombyx mori.";
RL J. Biol. Chem. 271:13854-13860(1996).
CC -!- FUNCTION: Binds specifically to peptidoglycan and triggers the
CC propenoloxidase cascade which is an important insect defense mechanism.
CC {ECO:0000269|PubMed:8662762}.
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:8662762}.
CC -!- TISSUE SPECIFICITY: Constitutively expressed in fat body, epithelial
CC cells and hemocytes. Not detected in Malpighian tubules, silk gland or
CC midgut. {ECO:0000269|PubMed:10207004}.
CC -!- INDUCTION: By bacterial challenge. {ECO:0000269|PubMed:10207004}.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000305}.
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DR EMBL; AB016605; BAA77210.1; -; Genomic_DNA.
DR EMBL; AB016249; BAA77209.1; -; mRNA.
DR RefSeq; NP_001036836.1; NM_001043371.1.
DR AlphaFoldDB; Q9XTN0; -.
DR SMR; Q9XTN0; -.
DR STRING; 7091.BGIBMGA008038-TA; -.
DR GeneID; 692372; -.
DR KEGG; bmor:692372; -.
DR CTD; 692372; -.
DR eggNOG; ENOG502S2KY; Eukaryota.
DR HOGENOM; CLU_037559_3_2_1; -.
DR OrthoDB; 1110472at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0042834; F:peptidoglycan binding; ISS:UniProtKB.
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 Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:10207004,
FT ECO:0000269|PubMed:8662762"
FT CHAIN 24..196
FT /note="Peptidoglycan recognition protein"
FT /id="PRO_0000023904"
FT DOMAIN 46..173
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000255"
FT DISULFID 25..147
FT /evidence="ECO:0000255"
FT DISULFID 61..67
FT /evidence="ECO:0000255"
SQ SEQUENCE 196 AA; 21627 MW; 225AD76EC24DA900 CRC64;
MARLHSAVVL ALALSSLLTE IAADCDVVSK KQWDGLIPVH VSYLARPVSL VIVQHTVTPF
CRTDAGCEEL VRNIQTNHME ALQYWDIGPS FLVGGNGKVY EGSGWLHVGA HTYGYNSRSI
GVAFIGNFNT DEPSGAMLEA LRSLLRCGVE RGHLAGDYRA VAHRQLIASE SPGRKLYNQI
RRWPEWLENV DSIKNA