Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9VV96 (PGSB2_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. 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 SB2

EC=3.5.1.28
Gene names
Name:PGRP-SB2
ORF Names:CG9697
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length182 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). Probably plays a scavenger role by digesting biologically active PGN into biologically inactive fragments. Has no direct bacteriolytic activity By similarity.

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 Potential.

Developmental stage

Not expressed in adults. Ref.4

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 182165Peptidoglycan-recognition protein SB2
PRO_0000023908

Sites

Metal binding481Zinc By similarity
Metal binding811Zinc By similarity
Metal binding1551Zinc By similarity
Metal binding1631Zinc By similarity

Amino acid modifications

Glycosylation1491N-linked (GlcNAc...) Potential
Disulfide bond54 ↔ 60 By similarity

Natural variations

Natural variant151A → V in strain: ZW141.
Natural variant511T → A in strain: Loua.
Natural variant621L → S in strain: ZW141.
Natural variant1521V → L in strain: Draveil, Loua, Monty5, P.bourg, Tahiti, Texas and ZW141.

Sequences

Sequence LengthMass (Da)Tools
Q9VV96 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 99AC18AD426BC308

FASTA18220,459
        10         20         30         40         50         60 
MKLQLALVLC GLTLALGQIV PRSSWCPVPI SPRMPRLMVP VRLIIIHHTV TAPCFNPHQC 

        70         80         90        100        110        120 
QLVLRQIRAD HMRRKFRDIG YNFLIGGDGR IYEGLGFGIR GEHAPRYNSQ SIGIAFIGNF 

       130        140        150        160        170        180 
QTGLPPSQML QAARTLIQIA VQRRQVSPNY SVVGHCQTKA TACPGIHLLN ELKKWPNWRP 


KP 

« 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].
Strain: DI7, Draveil, KY024, KY038, Loua, Monty5, P.bourg, S30, Tahiti, Texas and ZW141.
[2]"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.
[3]"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.
[4]"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: IDENTIFICATION, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ556575 Genomic DNA. Translation: CAD89140.1.
AJ556576 Genomic DNA. Translation: CAD89141.1.
AJ556577 Genomic DNA. Translation: CAD89142.1.
AJ556578 Genomic DNA. Translation: CAD89143.1.
AJ556579 Genomic DNA. Translation: CAD89144.1.
AJ556580 Genomic DNA. Translation: CAD89145.1.
AJ556581 Genomic DNA. Translation: CAD89146.1.
AJ556582 Genomic DNA. Translation: CAD89147.1.
AJ556583 Genomic DNA. Translation: CAD89148.1.
AJ556584 Genomic DNA. Translation: CAD89149.1.
AJ556585 Genomic DNA. Translation: CAD89150.1.
AE014296 Genomic DNA. Translation: AAF49421.1.
RefSeqNP_648916.1. NM_140659.3.
UniGeneDm.24013.

3D structure databases

ProteinModelPortalQ9VV96.
SMRQ9VV96. Positions 40-182.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9VV96.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0075320; FBpp0075079; FBgn0043577.
GeneID39869.
KEGGdme:Dmel_CG9697.
UCSCCG9697-RA. d. melanogaster.

Organism-specific databases

CTD39869.
FlyBaseFBgn0043577. PGRP-SB2.

Phylogenomic databases

eggNOGNOG241935.
GeneTreeENSGT00390000016833.
InParanoidQ9VV96.
KOK01446.
OrthoDBEOG757CZ5.
PhylomeDBQ9VV96.

Gene expression databases

BgeeQ9VV96.

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

GenomeRNAi39869.
NextBio815800.

Entry information

Entry namePGSB2_DROME
AccessionPrimary (citable) accession number: Q9VV96
Secondary accession number(s): Q70PX1, Q70PX3, Q70PX5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 92 of the entry and version 1 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