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P31178 (GLE_CHLRE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Autolysin
EC=3.4.24.38
Alternative name(s):
Gamete lytic enzyme
Short name=GLE
Gametolysin
OrganismChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifier3055 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Chlorophyta › Chlorophyceae › Chlamydomonadales › Chlamydomonadaceae › Chlamydomonas

Protein attributes

Sequence length638 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates digestion of the cell walls of the 2 mating type gametes during mating as a necessary prelude to cell fusion. This enzyme acts specifically on the framework proteins (inner wall) of the cell wall, cleaving several model peptides at specific sites.

Catalytic activity

Cleavage of the proline- and hydroxyproline-rich proteins of the Chlamydomonas cell wall; also cleaves azocasein, gelatin and Leu-Trp-Met-|-Arg-Phe-Ala.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Periplasm. Secreted › cell wall. Note: Stored in the periplasm of gametes until its release. Secreted concurrently with release of the cell walls.

Induction

By the signal of flagellar agglutination between gametes of the opposite mating type.

Domain

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Post-translational modification

Present in 2 forms: an inactive V-form in vegetative cells and an active and soluble G-form. The V-form enzyme may be converted to the G-form enzyme during gametic differentiation under nitrogen-starved conditions.

Sequence similarities

Belongs to the peptidase M11 family.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentCell wall
Periplasm
Secreted
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMGlycoprotein
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processcellular cell wall organization

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcell wall

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular matrix

Inferred from electronic annotation. Source: InterPro

periplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Propeptide29 – 183155Activation peptide
PRO_0000028870
Chain184 – 638455Autolysin
PRO_0000028871

Regions

Motif95 – 1028Cysteine switch By similarity
Compositional bias49 – 6214Pro-rich
Compositional bias271 – 28313Pro-rich

Sites

Active site3971 By similarity
Metal binding971Zinc; in inhibited form By similarity
Metal binding3961Zinc; catalytic By similarity
Metal binding4001Zinc; catalytic By similarity
Metal binding4061Zinc; catalytic By similarity

Amino acid modifications

Glycosylation301N-linked (GlcNAc...) Potential
Glycosylation1261N-linked (GlcNAc...) Potential
Glycosylation2961N-linked (GlcNAc...) Potential
Glycosylation4581N-linked (GlcNAc...) Potential
Glycosylation4651N-linked (GlcNAc...) Potential
Glycosylation4701N-linked (GlcNAc...) Potential
Glycosylation5231N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P31178 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: D3E3467701177251

FASTA63869,833
        10         20         30         40         50         60 
MSLATRRFGA AAALLVAACV LCTAPAWAQN ETTGTGMVKT KSAFRWIRPP PARPPPFRRP 

        70         80         90        100        110        120 
PPAQTPYVHK VEYTELQILC PQTIDSVTGY PMDDPRCNVP RATVAAGEEA LTIRNEFELL 

       130        140        150        160        170        180 
NGDVLNVTLE EVDTPENPSR RRLLSIIREE QRTGRVLLAT SAELPTPTFR LKSLKSILKG 

       190        200        210        220        230        240 
SQKEIYAGKP IDLRTIVYIM DFSSCKLSGW SAPATLTPEK VTSDMLRGAS APTNNLANYY 

       250        260        270        280        290        300 
GACSYEKTLF NPDNFLVLGP VPVPCIGGVT PPPRPPRPPR PPPRAGSTIS SLSRRNDTYD 

       310        320        330        340        350        360 
DWWDLSKYCT ASEQQAWERA AEAYAQAIVA QDPNSATGKK LQGILQWRER RRNIYILPPG 

       370        380        390        400        410        420 
VKCSWSGYAD VTCTSATCSA YVRGYSDTNA MQVIMHEAMH NYGLEHAGRG TLEYGDATDV 

       430        440        450        460        470        480 
MGDFNKAGKG LLCPNAPNMY RIGWAKPINE PGVAPFQNAT GAWGNLTAAN FTTDPWIRGL 

       490        500        510        520        530        540 
VIPAQGTRDD NMIVVNVGAQ STRDGAMKAT GAQAYYFSYR IKNTTAGGYD SGLTLDFHKK 

       550        560        570        580        590        600 
VLVHAYNGIQ SERVFGFKSN LLDWGPNFQS RSNTWTSPFL AYNNGLGGGV RLVVQSTSDT 

       610        620        630 
QAVVDICRIS ENGKELSCDD GIDNDCDGLQ DNEDPDCQ

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References

[1]"Primary structure and expression of a gamete lytic enzyme in Chlamydomonas reinhardtii: similarity of functional domains to matrix metalloproteases."
Kinoshita T., Fukuzawa H., Shimada T., Saito T., Matsuda Y.
Proc. Natl. Acad. Sci. U.S.A. 89:4693-4697(1992) [PubMed: 1584806] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 184-203.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M94265 mRNA. Translation: AAA33094.1.
D10542 mRNA. Translation: BAA01400.1.
PIRA45287.

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPSM11.001.

Proteomic databases

PRIDEP31178.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR021158. Pept_M10A_Zn_BS.
IPR008752. Peptidase_M11.
IPR016517. Peptidase_M11_autolysin.
[Graphical view]
PfamPF05548. Peptidase_M11. 1 hit.
[Graphical view]
PIRSFPIRSF007635. Autolysin. 1 hit.
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00142. ZINC_PROTEASE. False negative.
[Graphical view]
ProtoNetSearch...

Other

PMAP-CutDBP31178.

Entry information

Entry nameGLE_CHLRE
AccessionPrimary (citable) accession number: P31178
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 16, 2011
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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