ID E2C4B7_HARSA Unreviewed; 450 AA.
AC E2C4B7;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Peptidoglycan-recognition protein-LF {ECO:0000313|EMBL:EFN77212.1};
GN ORFNames=EAI_12691 {ECO:0000313|EMBL:EFN77212.1};
OS Harpegnathos saltator (Jerdon's jumping ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN [1] {ECO:0000313|EMBL:EFN77212.1, ECO:0000313|Proteomes:UP000008237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN77212.1,
RC ECO:0000313|Proteomes:UP000008237};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000256|ARBA:ARBA00007553}.
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DR EMBL; GL452440; EFN77212.1; -; Genomic_DNA.
DR RefSeq; XP_011150485.1; XM_011152183.2.
DR RefSeq; XP_011150486.1; XM_011152184.2.
DR AlphaFoldDB; E2C4B7; -.
DR EnsemblMetazoa; XM_011152183.3; XP_011150485.1; LOC105189832.
DR EnsemblMetazoa; XM_011152184.3; XP_011150486.1; LOC105189832.
DR GeneID; 105189832; -.
DR KEGG; hst:105189832; -.
DR InParanoid; E2C4B7; -.
DR OMA; TQSECTF; -.
DR OrthoDB; 2282228at2759; -.
DR PhylomeDB; E2C4B7; -.
DR Proteomes; UP000008237; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; 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; IPR015510; PGRP.
DR InterPro; IPR006619; PGRP_domain_met/bac.
DR PANTHER; PTHR11022:SF66; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR PANTHER; PTHR11022; PEPTIDOGLYCAN RECOGNITION PROTEIN; 1.
DR Pfam; PF01510; Amidase_2; 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 Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008237};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 230..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 284..427
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT DOMAIN 298..433
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..100
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 450 AA; 48846 MW; 3AFAD0C1F5C7200C CRC64;
MVTLVQQQQT PDDSHQCQKE EQERADGAVV VAESHAVVGD FHGEKEQEEE EAEVARRANE
IALVVPGNDS VGGSSTQCSD IDDDDVEDDE DEDEEETDVE DGRGGNGRGG GGWVANLPVP
AAIVQQHQEV ATANGDVVLP NADPSNFGDV CVKNSTNVHL GNKTFYKGPV TIKQFVYTSP
ASVQDANKLE AGSQASDANV SDLSSKVDVG ANRPILQQNS ELDKVTQWLW TWRCAALLCT
LALILVTAVV VCSLYLTRRA DAPAAPVFPE IPDSSLVGVE VTSVRFVERN EWGAQPPSQP
LTRLKLPVPY VIISHTATDF CTTQSECTFH VRFAQTFHIE SRKWSDIGYN FLVGGDGLAY
VGRSWDYVGA HSFGFNNRSI GISFIGTFNS VIPPKVQLHA AQKIIELGVK AGKIAPDYKL
LGHRQISKTL SPGDALYSIL KTWPHWVPAP
//
