SC1B_DROME
ID SC1B_DROME Reviewed; 185 AA.
AC C0HK99; A0A0B4LEX8; B5RJ78; Q2XY86; Q70PU9; Q70PV0; Q95SQ9; Q9V3B7;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Peptidoglycan-recognition protein SC1b {ECO:0000303|PubMed:11106397};
DE EC=3.5.1.28 {ECO:0000269|PubMed:12496260};
DE Flags: Precursor;
GN Name=PGRP-SC1b {ECO:0000303|PubMed:11106397,
GN ECO:0000312|FlyBase:FBgn0033327};
GN ORFNames=CG8577 {ECO:0000312|FlyBase:FBgn0033327};
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 [MRNA], FUNCTION, PGN-BINDING, TISSUE SPECIFICITY, AND
RP 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DI7, Draveil, KY038, Loua, P.bourg, S14, S30, Tahiti, and Texas;
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 [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; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, ENZYME ACTIVITY, COFACTOR, PGN-BINDING, AND MUTAGENESIS OF
RP CYS-168.
RX PubMed=12496260; DOI=10.1074/jbc.m208900200;
RA Mellroth P., Karlsson J., Steiner H.;
RT "A scavenger function for a Drosophila peptidoglycan recognition protein.";
RL J. Biol. Chem. 278:7059-7064(2003).
CC -!- FUNCTION: N-acetylmuramyl-L-alanine amidase involved in innate immunity
CC by degrading bacterial peptidoglycans (PGN) (PubMed:11106397,
CC PubMed:12496260). Plays a scavenger role by digesting biologically
CC active PGN into biologically inactive fragments (PubMed:12496260). Has
CC no direct bacteriolytic activity (PubMed:12496260).
CC {ECO:0000269|PubMed:11106397, ECO:0000269|PubMed:12496260}.
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 Evidence={ECO:0000269|PubMed:12496260};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000305|PubMed:12496260};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Constitutively expressed at high level in gut, in
CC addition to the induced expression in fat body.
CC {ECO:0000269|PubMed:11106397}.
CC -!- INDUCTION: Up-regulated by PGN from B.subtilis.
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=AAL28193.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF207542; AAG23736.1; -; mRNA.
DR EMBL; AE013599; AAF59052.1; -; Genomic_DNA.
DR EMBL; AE013599; AHN56007.1; -; Genomic_DNA.
DR EMBL; AJ556599; CAD89164.1; -; Genomic_DNA.
DR EMBL; AJ556600; CAD89165.1; -; Genomic_DNA.
DR EMBL; AJ556602; CAD89167.1; -; Genomic_DNA.
DR EMBL; AJ556604; CAD89169.1; -; Genomic_DNA.
DR EMBL; AJ556605; CAD89170.1; -; Genomic_DNA.
DR EMBL; AJ556606; CAD89171.1; -; Genomic_DNA.
DR EMBL; AJ556607; CAD89172.1; -; Genomic_DNA.
DR EMBL; AJ556608; CAD89173.1; -; Genomic_DNA.
DR EMBL; AJ556609; CAD89174.1; -; Genomic_DNA.
DR EMBL; AY060645; AAL28193.2; ALT_INIT; mRNA.
DR EMBL; BT044352; ACH92417.2; -; mRNA.
DR RefSeq; NP_001286209.1; NM_001299280.1.
DR RefSeq; NP_610407.1; NM_136563.2.
DR RefSeq; NP_610409.1; NM_136565.2.
DR AlphaFoldDB; C0HK99; -.
DR SMR; C0HK99; -.
DR DNASU; 35861; -.
DR EnsemblMetazoa; FBtr0088707; FBpp0087786; FBgn0043576.
DR EnsemblMetazoa; FBtr0088708; FBpp0087787; FBgn0033327.
DR EnsemblMetazoa; FBtr0339336; FBpp0308436; FBgn0033327.
DR GeneID; 35859; -.
DR GeneID; 35861; -.
DR KEGG; dme:Dmel_CG14746; -.
DR KEGG; dme:Dmel_CG8577; -.
DR CTD; 35859; -.
DR CTD; 35861; -.
DR FlyBase; FBgn0033327; PGRP-SC1b.
DR VEuPathDB; VectorBase:FBgn0033327; -.
DR VEuPathDB; VectorBase:FBgn0043576; -.
DR GeneTree; ENSGT00940000166535; -.
DR OMA; FMKQFAI; -.
DR OrthoDB; 1110472at2759; -.
DR BioGRID-ORCS; 35859; 0 hits in 3 CRISPR screens.
DR BioGRID-ORCS; 35861; 0 hits in 3 CRISPR screens.
DR PRO; PR:C0HK99; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033327; Expressed in midgut and 7 other tissues.
DR ExpressionAtlas; C0HK99; baseline and differential.
DR GO; GO:0005576; C:extracellular region; ISS:FlyBase.
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; TAS:FlyBase.
DR GO; GO:0002814; P:negative regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria; IGI:FlyBase.
DR GO; GO:0061060; P:negative regulation of peptidoglycan recognition protein signaling pathway; IDA:FlyBase.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IDA:FlyBase.
DR GO; GO:0045752; P:positive regulation of Toll signaling pathway; IMP: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 1: Evidence at protein level;
KW Disulfide bond; Hydrolase; Immunity; Innate immunity; Metal-binding;
KW Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..185
FT /note="Peptidoglycan-recognition protein SC1b"
FT /id="PRO_0000438897"
FT DOMAIN 46..170
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000255"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:12496260"
FT SITE 86
FT /note="Essential for zinc hydrate coordination"
FT /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT DISULFID 58..64
FT /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT VARIANT 6
FT /note="A -> T (in strain: KY038)"
FT MUTAGEN 168
FT /note="C->A: Abolishes enzyme activity but retains PGN-
FT binding."
FT /evidence="ECO:0000269|PubMed:12496260"
FT CONFLICT 178
FT /note="R -> P (in Ref. 5; AAL28193)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 185 AA; 20395 MW; F23F8D80A33541AC CRC64;
MVSKVALLLA VLVCSQYMAQ GVYVVSKAEW GGRGAKWTVG LGNYLSYAII HHTAGSYCET
RAQCNAVLQS VQNYHMDSLG WPDIGYNFLI GGDGNVYEGR GWNNMGAHAA EWNPYSIGIS
FLGNYNWDTL EPNMISAAQQ LLNDAVNRGQ LSSGYILYGH RQVSATECPG THIWNEIRGW
SHWSG
