PGSB1_DROME
ID PGSB1_DROME Reviewed; 190 AA.
AC Q70PY2; A0FIQ1; A0JQ53; Q4V3W6; Q70PY3; Q70PY4; Q70PY7; Q9VV97;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Peptidoglycan-recognition protein SB1;
DE EC=3.5.1.28;
DE Flags: Precursor;
GN Name=PGRP-SB1; ORFNames=CG9681;
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], AND VARIANTS LEU-9; ALA-36 AND ALA-113.
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 [MRNA], FUNCTION, AND VARIANT ALA-113.
RC TISSUE=Embryo;
RX PubMed=17046713; DOI=10.1016/j.bbrc.2006.09.139;
RA Mellroth P., Steiner H.;
RT "PGRP-SB1: an N-acetylmuramoyl L-alanine amidase with antibacterial
RT activity.";
RL Biochem. Biophys. Res. Commun. 350:994-999(2006).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Kapadia B.,
RA Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
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), preferentially DAP-type
CC PGNs. Probably plays a scavenger role by digesting biologically active
CC PGN into biologically inactive fragments.
CC {ECO:0000269|PubMed:17046713}.
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:0000269|PubMed:11106397}.
CC -!- TISSUE SPECIFICITY: In larvae, it is mainly expressed in fat body.
CC {ECO:0000269|PubMed:11106397}.
CC -!- INDUCTION: Strongly up-regulated by PGN from B.subtilis. Weakly or not
CC expressed in normal conditions. Regulated by the imd/Relish pathway.
CC {ECO:0000269|PubMed:11106397}.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK57080.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ556563; CAD89128.1; -; Genomic_DNA.
DR EMBL; AJ556564; CAD89129.1; -; Genomic_DNA.
DR EMBL; AJ556565; CAD89130.1; -; Genomic_DNA.
DR EMBL; AJ556566; CAD89131.1; -; Genomic_DNA.
DR EMBL; AJ556567; CAD89132.1; -; Genomic_DNA.
DR EMBL; AJ556568; CAD89133.1; -; Genomic_DNA.
DR EMBL; AJ556569; CAD89134.1; -; Genomic_DNA.
DR EMBL; AJ556570; CAD89135.1; -; Genomic_DNA.
DR EMBL; AJ556571; CAD89136.1; -; Genomic_DNA.
DR EMBL; AJ556572; CAD89137.1; -; Genomic_DNA.
DR EMBL; AJ556573; CAD89138.1; -; Genomic_DNA.
DR EMBL; EF011112; ABJ98404.1; -; mRNA.
DR EMBL; AE014296; AAF49420.1; -; Genomic_DNA.
DR EMBL; BT023240; AAY55656.1; -; mRNA.
DR EMBL; BT029423; ABK57080.1; ALT_INIT; mRNA.
DR RefSeq; NP_648917.1; NM_140660.4.
DR AlphaFoldDB; Q70PY2; -.
DR SMR; Q70PY2; -.
DR STRING; 7227.FBpp0075107; -.
DR GlyGen; Q70PY2; 3 sites.
DR PaxDb; Q70PY2; -.
DR PRIDE; Q70PY2; -.
DR DNASU; 39870; -.
DR EnsemblMetazoa; FBtr0075348; FBpp0075107; FBgn0043578.
DR GeneID; 39870; -.
DR KEGG; dme:Dmel_CG9681; -.
DR CTD; 39870; -.
DR FlyBase; FBgn0043578; PGRP-SB1.
DR VEuPathDB; VectorBase:FBgn0043578; -.
DR eggNOG; ENOG502QR3D; Eukaryota.
DR GeneTree; ENSGT00940000166535; -.
DR HOGENOM; CLU_037559_3_2_1; -.
DR InParanoid; Q70PY2; -.
DR OMA; SDQCKRM; -.
DR OrthoDB; 1110472at2759; -.
DR PhylomeDB; Q70PY2; -.
DR BRENDA; 3.5.1.28; 1994.
DR BioGRID-ORCS; 39870; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39870; -.
DR PRO; PR:Q70PY2; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0043578; Expressed in mouthpart and 16 other tissues.
DR Genevisible; Q70PY2; DM.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IDA: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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..190
FT /note="Peptidoglycan-recognition protein SB1"
FT /id="PRO_0000023907"
FT DOMAIN 47..174
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000255"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT SITE 90
FT /note="Important for catalytic activity; essential for
FT amidase activity and zinc hydrate coordination"
FT /evidence="ECO:0000250|UniProtKB:P00806"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..68
FT /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT VARIANT 9
FT /note="F -> L (in strain: DI7, KY038 and Loua)"
FT /evidence="ECO:0000269|PubMed:14738318"
FT VARIANT 36
FT /note="V -> A (in strain: DI7, Loua and S30)"
FT /evidence="ECO:0000269|PubMed:14738318"
FT VARIANT 113
FT /note="S -> A (in strain: DI7, Loua, Monty5, Tahiti and
FT ZW141)"
FT /evidence="ECO:0000269|PubMed:14738318,
FT ECO:0000269|PubMed:17046713"
SQ SEQUENCE 190 AA; 20998 MW; A2F81E4903E8173E CRC64;
MNTSTAISFV AALVLCCLAL SANALQIEPR SSWGAVSARS PSRISGAVDY VIIHHSDNPN
GCSTSEQCKR MIKNIQSDHK GRRNFSDIGY NFIVAGDGKV YEGRGFGLQG SHSPNYNRKS
IGIVFIGNFE RSAPSAQMLQ NAKDLIELAK QRGYLKDNYT LFGHRQTKAT SCPGDALYNE
IKTWPHWRQN
