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Q70PY2 (PGSB1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidoglycan-recognition protein SB1

EC=3.5.1.28
Gene names
Name:PGRP-SB1
ORF Names:CG9681
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length190 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN), preferentially DAP-type PGNs. Probably plays a scavenger role by digesting biologically active PGN into biologically inactive fragments. Ref.2

Catalytic activity

Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.

Cofactor

Zinc By similarity.

Subcellular location

Secreted Ref.6.

Tissue specificity

In larvae, it is mainly expressed in fat body. Ref.6

Induction

Strongly up-regulated by PGN from B.subtilis. Weakly or not expressed in normal conditions. Regulated by the imd/Relish pathway. Ref.6

Sequence similarities

Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.

Sequence caution

The sequence ABK57080.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 190166Peptidoglycan-recognition protein SB1
PRO_0000023907

Sites

Metal binding551Zinc By similarity
Metal binding901Zinc By similarity
Metal binding1641Zinc By similarity
Metal binding1721Zinc By similarity

Amino acid modifications

Glycosylation21N-linked (GlcNAc...) Potential
Glycosylation841N-linked (GlcNAc...) Potential
Glycosylation1581N-linked (GlcNAc...) Potential
Disulfide bond62 ↔ 68 By similarity

Natural variations

Natural variant91F → L in strain: DI7, KY038 and Loua. Ref.1
Natural variant361V → A in strain: DI7, Loua and S30. Ref.1
Natural variant1131S → A in strain: DI7, Loua, Monty5, Tahiti and ZW141. Ref.1 Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q70PY2 [UniParc].

Last modified May 10, 2005. Version 2.
Checksum: A2F81E4903E8173E

FASTA19020,998
        10         20         30         40         50         60 
MNTSTAISFV AALVLCCLAL SANALQIEPR SSWGAVSARS PSRISGAVDY VIIHHSDNPN 

        70         80         90        100        110        120 
GCSTSEQCKR MIKNIQSDHK GRRNFSDIGY NFIVAGDGKV YEGRGFGLQG SHSPNYNRKS 

       130        140        150        160        170        180 
IGIVFIGNFE RSAPSAQMLQ NAKDLIELAK QRGYLKDNYT LFGHRQTKAT SCPGDALYNE 

       190 
IKTWPHWRQN 

« Hide

References

« Hide 'large scale' references
[1]"The evolution of parasite recognition genes in the innate immune system: purifying selection on Drosophila melanogaster peptidoglycan recognition proteins."
Jiggins F.M., Hurst G.D.D.
J. Mol. Evol. 57:598-605(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-9; ALA-36 AND ALA-113.
Strain: DI7, Draveil, KY024, KY038, Loua, Monty5, P.bourg, S30, Tahiti, Texas and ZW141.
[2]"PGRP-SB1: an N-acetylmuramoyl L-alanine amidase with antibacterial activity."
Mellroth P., Steiner H.
Biochem. Biophys. Res. Commun. 350:994-999(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, VARIANT ALA-113.
Tissue: Embryo.
[3]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[5]Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Kapadia B., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
[6]"A family of peptidoglycan recognition proteins in the fruit fly Drosophila melanogaster."
Werner T., Liu G., Kang D., Ekengren S., Steiner H., Hultmark D.
Proc. Natl. Acad. Sci. U.S.A. 97:13772-13777(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ556563 Genomic DNA. Translation: CAD89128.1.
AJ556564 Genomic DNA. Translation: CAD89129.1.
AJ556565 Genomic DNA. Translation: CAD89130.1.
AJ556566 Genomic DNA. Translation: CAD89131.1.
AJ556567 Genomic DNA. Translation: CAD89132.1.
AJ556568 Genomic DNA. Translation: CAD89133.1.
AJ556569 Genomic DNA. Translation: CAD89134.1.
AJ556570 Genomic DNA. Translation: CAD89135.1.
AJ556571 Genomic DNA. Translation: CAD89136.1.
AJ556572 Genomic DNA. Translation: CAD89137.1.
AJ556573 Genomic DNA. Translation: CAD89138.1.
EF011112 mRNA. Translation: ABJ98404.1.
AE014296 Genomic DNA. Translation: AAF49420.1.
BT023240 mRNA. Translation: AAY55656.1.
BT029423 mRNA. Translation: ABK57080.1. Different initiation.
RefSeqNP_648917.1. NM_140660.4.
UniGeneDm.24753.

3D structure databases

ProteinModelPortalQ70PY2.
SMRQ70PY2. Positions 30-189.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ70PY2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0075348; FBpp0075107; FBgn0043578.
GeneID39870.
KEGGdme:Dmel_CG9681.

Organism-specific databases

CTD39870.
FlyBaseFBgn0043578. PGRP-SB1.

Phylogenomic databases

eggNOGCOG5479.
GeneTreeENSGT00390000016833.
InParanoidQ70PY2.
KOK01446.
OMANEIKTWP.
OrthoDBEOG757CZ5.
PhylomeDBQ70PY2.

Enzyme and pathway databases

BRENDA3.5.1.28. 1994.

Gene expression databases

BgeeQ70PY2.

Family and domain databases

Gene3D3.40.80.10. 1 hit.
InterProIPR002502. Amidase_domain.
IPR017331. Peptidoglycan_recognition.
IPR015510. PGRP.
IPR006619. PGRP_domain_met/bac.
[Graphical view]
PANTHERPTHR11022. PTHR11022. 1 hit.
PfamPF01510. Amidase_2. 1 hit.
[Graphical view]
PIRSFPIRSF037945. PGRPs. 1 hit.
SMARTSM00644. Ami_2. 1 hit.
SM00701. PGRP. 1 hit.
[Graphical view]
SUPFAMSSF55846. SSF55846. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi39870.
NextBio815805.

Entry information

Entry namePGSB1_DROME
AccessionPrimary (citable) accession number: Q70PY2
Secondary accession number(s): A0FIQ1 expand/collapse secondary AC list , A0JQ53, Q4V3W6, Q70PY3, Q70PY4, Q70PY7, Q9VV97
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 10, 2005
Last modified: July 9, 2014
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase