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Reviewed, UniProtKB/Swiss-Prot Q5HN75 (GSEA_STAEQ)

Last modified January 19, 2010. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutamyl endopeptidase
    EC=3.4.21.19
Alternative name(s):
    Glutamic acid-specific protease
      Short name=GluSE
Gene names
Name: gseA
Ordered Locus Names: SERP1397
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Exhibits a significant hydrolytic activity for the carbonyl side of glutamic acid. Shows activity toward human fibronectin and type 1 collagen By similarity.

Catalytic activity

Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the peptidase S1B family.

Ontologies

Keywords
   Biological processVirulence
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMZymogen
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Propeptide28 – 6639 By similarity
PRO_0000026898
Chain67 – 282216Glutamyl endopeptidase
PRO_0000026899

Sites

Active site1171Charge relay system By similarity
Active site1591Charge relay system By similarity
Active site2351Charge relay system By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HN75-1 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 5DA679C179F8A787

FASTA28230,831
        10         20         30         40         50         60 
MKKRFLSICT MTIAALATTT MVNTSYAKTD TESHNHSSLG TENKNVLDIN SSSHNIKPSQ 

        70         80         90        100        110        120 
NKSYPSVILP NNNRHQIFNT TQGHYDAVSF IYIPIHGGYM SGSGVVVGEN EILTNKHVVN 

       130        140        150        160        170        180 
GAKGNPRNIS VHPSAKNEND YPNGKFVGQE IIPYPGNSDL AILRVSPNEH NQHIGQVVKP 

       190        200        210        220        230        240 
ATISSNTDTR INENITVTGY PGDKPLATMW ESVGKVVYIG GEELRYDLST VGGNSGSPVF 

       250        260        270        280 
NGKNQVIGIH YGGVDNKYNS SVYINDFVQQ FLRNNIPDIN IQ 

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000029 Genomic DNA. Translation: AAW54738.1.
RefSeqYP_188966.1.

3D structure databases

SMRQ5HN75. Positions 67-281.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HN75.

Genome annotation databases

GeneID3240839.
GenomeReviewsGene locus SERP1397 in contig CP000029_GR.
KEGGser:SERP1397.
NMPDRfig|176279.3.peg.1366.
TIGRSERP1397.

Phylogenomic databases

eggNOGCOG3591.
HOGENOMHBG693141.
OMAEDINFAN.

Enzyme and pathway databases

BioCycSEPI176279:SERP1397-MONOMER.

Family and domain databases

InterProIPR000126. Pept_S1B_AS.
IPR001254. Peptidase_S1_S6.
IPR008256. Peptidase_S1B.
IPR008353. Peptidase_S1B_tx.
IPR009003. Ser/Cys_Pept_Trypsin-like.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR01774. EXFOLTOXIN.
PR00839. V8PROTEASE.
PROSITEPS00672. V8_HIS. False negative.
PS00673. V8_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSEA_STAEQ
AccessionPrimary (citable) accession number: Q5HN75
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: February 15, 2005
Last modified: January 19, 2010
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents