PGSB2_DROME
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 03-AUG-2022, entry version 140.
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 GlyGen; Q9VV96; 1 site.
DR PaxDb; Q9VV96; -.
DR DNASU; 39869; -.
DR EnsemblMetazoa; FBtr0075320; FBpp0075079; FBgn0043577.
DR GeneID; 39869; -.
DR KEGG; dme:Dmel_CG9697; -.
DR UCSC; CG9697-RA; d. melanogaster.
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 OMA; HCQTKAT; -.
DR OrthoDB; 1110472at2759; -.
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 tissues.
DR ExpressionAtlas; Q9VV96; baseline and differential.
DR Genevisible; Q9VV96; DM.
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; -; 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 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
