PGRP1_CAMDR
ID PGRP1_CAMDR Reviewed; 193 AA.
AC Q9GK12;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Peptidoglycan recognition protein 1;
DE AltName: Full=Peptidoglycan recognition protein short;
DE Short=PGRP-S;
DE Flags: Precursor;
GN Name=PGLYRP1; Synonyms=PGLYRP, PGRP;
OS Camelus dromedarius (Dromedary) (Arabian camel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX NCBI_TaxID=9838;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SIGNAL SEQUENCE, AND PROTEIN
RP SEQUENCE OF 22-26.
RC TISSUE=Lymphocyte;
RX PubMed=15328291; DOI=10.3168/jds.s0022-0302(04)73392-5;
RA Kappeler S.R., Heuberger C., Farah Z., Puhan Z.;
RT "Expression of the peptidoglycan recognition protein, PGRP, in the
RT lactating mammary gland.";
RL J. Dairy Sci. 87:2660-2668(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 23-193 IN COMPLEX WITH LPS AND
RP LTA, SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=21454594; DOI=10.1074/jbc.m111.228163;
RA Sharma P., Dube D., Singh A., Mishra B., Singh N., Sinha M., Dey S.,
RA Kaur P., Mitra D.K., Sharma S., Singh T.P.;
RT "Structural basis of recognition of pathogen-associated molecular patterns
RT and inhibition of proinflammatory cytokines by camel peptidoglycan
RT recognition protein.";
RL J. Biol. Chem. 286:16208-16217(2011).
CC -!- FUNCTION: Innate immunity protein that plays several important
CC functions in antimicrobial and antitumor defense systems. Acts as a
CC pattern receptor that binds to murein peptidoglycans (PGN) of Gram-
CC positive bacteria and thus provides bactericidal activity. Forms an
CC equimolar complex with heat shock protein HSPA1A and induces programmed
CC cell death through apoptosis and necroptosis in tumor cell lines by
CC activating the TNFR1 receptor on the target cell membrane. In addition,
CC acts in complex with the Ca(2+)-binding protein S100A4 as a
CC chemoattractant able to induce lymphocyte movement. Mechanistically,
CC this complex acts as a ligand of the chemotactic receptors CCR5 and
CC CXCR3 which are present on the cells of the immune system. Promotes
CC also the activation of lymphocytes that become able to kill virus-
CC infected cells as well as tumor cells by modulating the spectrum of
CC their target-cell specificity. Induction of cytotoxicity on monocyte
CC surface requires interaction with TREM1 receptor.
CC {ECO:0000250|UniProtKB:O75594}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:21454594}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasmic granule
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000305}.
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DR EMBL; AJ131676; CAC19553.1; -; mRNA.
DR EMBL; AJ409286; CAC84130.1; -; Genomic_DNA.
DR RefSeq; XP_010996001.1; XM_010997699.1.
DR PDB; 2R2K; X-ray; 3.25 A; A/B/C/D=23-193.
DR PDB; 2R90; X-ray; 2.80 A; A/B/C/D=23-193.
DR PDB; 2Z9N; X-ray; 3.20 A; A/B/C/D=23-193.
DR PDB; 3C2X; X-ray; 1.83 A; A/B/C/D=23-193.
DR PDB; 3CG9; X-ray; 2.90 A; A/B/C/D=23-193.
DR PDB; 3COR; X-ray; 3.10 A; A/B/C/D=23-193.
DR PDB; 3CXA; X-ray; 3.40 A; A/B/C/D=23-193.
DR PDB; 3NG4; X-ray; 1.73 A; A/B/C/D=23-193.
DR PDB; 3NNO; X-ray; 2.90 A; A/B/C/D=23-193.
DR PDB; 3NW3; X-ray; 2.50 A; A/B/C/D=23-193.
DR PDB; 3O4K; X-ray; 2.11 A; A/B/C/D=23-193.
DR PDB; 3OGX; X-ray; 2.80 A; A/B/C/D=23-193.
DR PDB; 3QJ1; X-ray; 3.20 A; A/B/C/D=23-193.
DR PDB; 3QS0; X-ray; 2.50 A; A/B/C/D=23-193.
DR PDB; 3QV4; X-ray; 2.70 A; A/B/C/D=23-193.
DR PDB; 3RT4; X-ray; 1.70 A; A/B/C/D=23-193.
DR PDB; 3T2V; X-ray; 2.51 A; A/B/C/D=23-193.
DR PDB; 3T39; X-ray; 2.70 A; A/B/C/D=23-193.
DR PDB; 3TRU; X-ray; 3.20 A; A/B/C/D=23-193.
DR PDB; 3UIL; X-ray; 2.20 A; A/B/C/D=23-193.
DR PDB; 3UML; X-ray; 2.15 A; A/B/C/D=23-193.
DR PDB; 3UMQ; X-ray; 2.20 A; A/B/C/D=23-193.
DR PDB; 3USX; X-ray; 2.28 A; A/B/C/D=23-193.
DR PDB; 4FNN; X-ray; 2.24 A; A/B/C/D=23-193.
DR PDB; 4GF9; X-ray; 2.80 A; A/B/C/D=23-193.
DR PDB; 4OPP; X-ray; 2.30 A; A/B/C/D=23-193.
DR PDB; 4ORV; X-ray; 2.50 A; A/B/C/D=23-193.
DR PDB; 4OUG; X-ray; 2.46 A; A/B/C/D=23-193.
DR PDB; 4Q8S; X-ray; 2.09 A; A/B/C/D=23-193.
DR PDB; 4Q9E; X-ray; 2.31 A; A/B/C/D=23-193.
DR PDB; 5DWF; X-ray; 1.83 A; A/B/C/D=28-193.
DR PDB; 5E0A; X-ray; 2.60 A; A/B/C/D=23-193.
DR PDB; 5E0B; X-ray; 2.60 A; A/B/C/D=23-193.
DR PDB; 5XGY; X-ray; 2.45 A; A/B/C/D=23-193.
DR PDB; 6A89; X-ray; 2.11 A; A/B/C/D=27-193.
DR PDB; 6IDM; X-ray; 3.20 A; A/B/C/D=28-193.
DR PDB; 7DY5; X-ray; 2.30 A; A/B/C/D=23-193.
DR PDB; 7XFW; X-ray; 2.07 A; A/B/C/D=23-193.
DR PDB; 7XFX; X-ray; 2.28 A; A/B/C/D=23-193.
DR PDB; 7XFY; X-ray; 2.67 A; A/B/C/D=23-193.
DR PDBsum; 2R2K; -.
DR PDBsum; 2R90; -.
DR PDBsum; 2Z9N; -.
DR PDBsum; 3C2X; -.
DR PDBsum; 3CG9; -.
DR PDBsum; 3COR; -.
DR PDBsum; 3CXA; -.
DR PDBsum; 3NG4; -.
DR PDBsum; 3NNO; -.
DR PDBsum; 3NW3; -.
DR PDBsum; 3O4K; -.
DR PDBsum; 3OGX; -.
DR PDBsum; 3QJ1; -.
DR PDBsum; 3QS0; -.
DR PDBsum; 3QV4; -.
DR PDBsum; 3RT4; -.
DR PDBsum; 3T2V; -.
DR PDBsum; 3T39; -.
DR PDBsum; 3TRU; -.
DR PDBsum; 3UIL; -.
DR PDBsum; 3UML; -.
DR PDBsum; 3UMQ; -.
DR PDBsum; 3USX; -.
DR PDBsum; 4FNN; -.
DR PDBsum; 4GF9; -.
DR PDBsum; 4OPP; -.
DR PDBsum; 4ORV; -.
DR PDBsum; 4OUG; -.
DR PDBsum; 4Q8S; -.
DR PDBsum; 4Q9E; -.
DR PDBsum; 5DWF; -.
DR PDBsum; 5E0A; -.
DR PDBsum; 5E0B; -.
DR PDBsum; 5XGY; -.
DR PDBsum; 6A89; -.
DR PDBsum; 6IDM; -.
DR PDBsum; 7DY5; -.
DR PDBsum; 7XFW; -.
DR PDBsum; 7XFX; -.
DR PDBsum; 7XFY; -.
DR AlphaFoldDB; Q9GK12; -.
DR SMR; Q9GK12; -.
DR STRING; 9838.ENSCDRP00005016406; -.
DR PRIDE; Q9GK12; -.
DR OrthoDB; 1110472at2759; -.
DR EvolutionaryTrace; Q9GK12; -.
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; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0001818; P:negative regulation of cytokine production; IDA:CACAO.
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 3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW Disulfide bond; Immunity; Innate immunity; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:15328291"
FT CHAIN 22..193
FT /note="Peptidoglycan recognition protein 1"
FT /id="PRO_0000023900"
FT DOMAIN 50..178
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000255"
FT DISULFID 28..152
FT /evidence="ECO:0000269|PubMed:21454594"
FT DISULFID 44..89
FT /evidence="ECO:0000269|PubMed:21454594"
FT DISULFID 65..71
FT /evidence="ECO:0000269|PubMed:21454594"
FT TURN 34..38
FT /evidence="ECO:0007829|PDB:3RT4"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:3RT4"
FT HELIX 68..84
FT /evidence="ECO:0007829|PDB:3RT4"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:3RT4"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:3RT4"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:3RT4"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:3RT4"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:3RT4"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:3RT4"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:3RT4"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:7XFW"
FT HELIX 140..155
FT /evidence="ECO:0007829|PDB:3RT4"
FT STRAND 158..167
FT /evidence="ECO:0007829|PDB:3RT4"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:3RT4"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:3RT4"
FT HELIX 179..185
FT /evidence="ECO:0007829|PDB:3RT4"
SQ SEQUENCE 193 AA; 21377 MW; B6A1BD818030A7CB CRC64;
MTRHCVLLVW ALLALLSLGA AREDPPACGS IVPRREWRAL ASECRERLTR PVRYVVVSHT
AGSHCDTPAS CAQQAQNVQS YHVRNLGWCD VGYNFLIGED GLVYEGRGWN IKGAHAGPTW
NPISIGISFM GNYMNRVPPP RALRAAQNLL ACGVALGALR SNYEVKGHRD VQPTLSPGDR
LYEIIQTWSH YRA
