ID   PGSB2_DROME             Reviewed;         182 AA.
AC   Q9VV96; Q70PX1; Q70PX3; Q70PX5;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 145.
DE   RecName: Full=Peptidoglycan-recognition protein SB2;
DE            EC=3.5.1.28;
DE   Flags: Precursor;
GN   Name=PGRP-SB2; ORFNames=CG9697;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DI7, Draveil, KY024, KY038, Loua, Monty5, P.bourg, S30, Tahiti,
RC   Texas, and ZW141;
RX   PubMed=14738318; DOI=10.1007/s00239-003-2506-6;
RA   Jiggins F.M., Hurst G.D.D.;
RT   "The evolution of parasite recognition genes in the innate immune system:
RT   purifying selection on Drosophila melanogaster peptidoglycan recognition
RT   proteins.";
RL   J. Mol. Evol. 57:598-605(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   IDENTIFICATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=11106397; DOI=10.1073/pnas.97.25.13772;
RA   Werner T., Liu G., Kang D., Ekengren S., Steiner H., Hultmark D.;
RT   "A family of peptidoglycan recognition proteins in the fruit fly Drosophila
RT   melanogaster.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:13772-13777(2000).
CC   -!- FUNCTION: N-acetylmuramyl-L-alanine amidase involved in innate immunity
CC       by degrading bacterial peptidoglycans (PGN). Probably plays a scavenger
CC       role by digesting biologically active PGN into biologically inactive
CC       fragments. Has no direct bacteriolytic activity (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC         amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q8INK6};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Not expressed in adults.
CC       {ECO:0000269|PubMed:11106397}.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ556575; CAD89140.1; -; Genomic_DNA.
DR   EMBL; AJ556576; CAD89141.1; -; Genomic_DNA.
DR   EMBL; AJ556577; CAD89142.1; -; Genomic_DNA.
DR   EMBL; AJ556578; CAD89143.1; -; Genomic_DNA.
DR   EMBL; AJ556579; CAD89144.1; -; Genomic_DNA.
DR   EMBL; AJ556580; CAD89145.1; -; Genomic_DNA.
DR   EMBL; AJ556581; CAD89146.1; -; Genomic_DNA.
DR   EMBL; AJ556582; CAD89147.1; -; Genomic_DNA.
DR   EMBL; AJ556583; CAD89148.1; -; Genomic_DNA.
DR   EMBL; AJ556584; CAD89149.1; -; Genomic_DNA.
DR   EMBL; AJ556585; CAD89150.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAF49421.1; -; Genomic_DNA.
DR   RefSeq; NP_648916.1; NM_140659.3.
DR   AlphaFoldDB; Q9VV96; -.
DR   SMR; Q9VV96; -.
DR   GlyCosmos; Q9VV96; 1 site, No reported glycans.
DR   GlyGen; Q9VV96; 1 site.
DR   DNASU; 39869; -.
DR   EnsemblMetazoa; FBtr0075320; FBpp0075079; FBgn0043577.
DR   GeneID; 39869; -.
DR   KEGG; dme:Dmel_CG9697; -.
DR   UCSC; CG9697-RA; d. melanogaster.
DR   AGR; FB:FBgn0043577; -.
DR   CTD; 39869; -.
DR   FlyBase; FBgn0043577; PGRP-SB2.
DR   VEuPathDB; VectorBase:FBgn0043577; -.
DR   GeneTree; ENSGT00940000166535; -.
DR   HOGENOM; CLU_037559_3_2_1; -.
DR   InParanoid; Q9VV96; -.
DR   PhylomeDB; Q9VV96; -.
DR   BioGRID-ORCS; 39869; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 39869; -.
DR   PRO; PR:Q9VV96; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0043577; Expressed in saliva-secreting gland and 7 other cell types or tissues.
DR   ExpressionAtlas; Q9VV96; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; ISS:FlyBase.
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; NAS:UniProtKB.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; ISS:FlyBase.
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:SF75; PEPTIDOGLYCAN-RECOGNITION PROTEIN LB-RELATED; 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.
DR   Genevisible; Q9VV96; DM.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Immunity; Innate immunity;
KW   Metal-binding; Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..182
FT                   /note="Peptidoglycan-recognition protein SB2"
FT                   /id="PRO_0000023908"
FT   DOMAIN          40..165
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000255"
FT   BINDING         47
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT   BINDING         155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT   BINDING         163
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT   SITE            81
FT                   /note="Important for catalytic activity; essential for
FT                   amidase activity and zinc hydrate coordination"
FT                   /evidence="ECO:0000250|UniProtKB:P00806"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        54..60
FT                   /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT   VARIANT         15
FT                   /note="A -> V (in strain: ZW141)"
FT   VARIANT         51
FT                   /note="T -> A (in strain: Loua)"
FT   VARIANT         62
FT                   /note="L -> S (in strain: ZW141)"
FT   VARIANT         152
FT                   /note="V -> L (in strain: Draveil, Loua, Monty5, P.bourg,
FT                   Tahiti, Texas and ZW141)"
SQ   SEQUENCE   182 AA;  20459 MW;  99AC18AD426BC308 CRC64;
     MKLQLALVLC GLTLALGQIV PRSSWCPVPI SPRMPRLMVP VRLIIIHHTV TAPCFNPHQC
     QLVLRQIRAD HMRRKFRDIG YNFLIGGDGR IYEGLGFGIR GEHAPRYNSQ SIGIAFIGNF
     QTGLPPSQML QAARTLIQIA VQRRQVSPNY SVVGHCQTKA TACPGIHLLN ELKKWPNWRP
     KP
//