ID A0A026WT18_OOCBI Unreviewed; 187 AA.
AC A0A026WT18;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Peptidoglycan-recognition protein {ECO:0000256|PIRNR:PIRNR037945};
GN ORFNames=X777_14995 {ECO:0000313|EMBL:EZA58826.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA58826.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA58826.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000256|ARBA:ARBA00007553, ECO:0000256|PIRNR:PIRNR037945}.
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DR EMBL; KK107119; EZA58826.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A026WT18; -.
DR STRING; 2015173.A0A026WT18; -.
DR EnsemblMetazoa; XM_020030642.2; XP_019886201.1; LOC105276273.
DR OMA; RFVVIHH; -.
DR OrthoDB; 2282228at2759; -.
DR Proteomes; UP000053097; 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};
KW Immunity {ECO:0000256|ARBA:ARBA00022859, ECO:0000256|PIRNR:PIRNR037945};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588,
KW ECO:0000256|PIRNR:PIRNR037945};
KW Reference proteome {ECO:0000313|Proteomes:UP000053097};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..187
FT /note="Peptidoglycan-recognition protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001541360"
FT DOMAIN 23..165
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT DOMAIN 34..171
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT DISULFID 22..145
FT /evidence="ECO:0000256|PIRSR:PIRSR037945-1"
FT DISULFID 59..65
FT /evidence="ECO:0000256|PIRSR:PIRSR037945-1"
SQ SEQUENCE 187 AA; 20759 MW; 3B6F5C0EA2D63607 CRC64;
MLSRVCLALL LLLPASLANV ECPKIIGRTQ WTSTPAGAVN YLIIPILYVV IHHTVTPECN
SRQECTSRVD GIRGYHMDDL GWDDIGYSFL IGGDGNVYEG CGWTREGAHT YGYNKKSIGI
AFIGNFQNKD ASQEMLNAAH KLIECGKDQG ILRSNVRVIG ARQVRQTSSP GNQLYEQIQD
WSEWSNP
//
