GLE_CHLRE
ID GLE_CHLRE Reviewed; 638 AA.
AC P31178;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Autolysin;
DE EC=3.4.24.38;
DE AltName: Full=Gamete lytic enzyme;
DE Short=GLE;
DE AltName: Full=Gametolysin;
DE Flags: Precursor;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 184-203.
RX PubMed=1584806; DOI=10.1073/pnas.89.10.4693;
RA Kinoshita T., Fukuzawa H., Shimada T., Saito T., Matsuda Y.;
RT "Primary structure and expression of a gamete lytic enzyme in Chlamydomonas
RT reinhardtii: similarity of functional domains to matrix metalloproteases.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:4693-4697(1992).
CC -!- FUNCTION: Mediates digestion of the cell walls of the 2 mating type
CC gametes during mating as a necessary prelude to cell fusion. This
CC enzyme acts specifically on the framework proteins (inner wall) of the
CC cell wall, cleaving several model peptides at specific sites.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of the proline- and hydroxyproline-rich proteins of
CC the Chlamydomonas cell wall. Also cleaves azocasein, gelatin and Leu-
CC Trp-Met-|-Arg-Phe-Ala.; EC=3.4.24.38;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Periplasm. Secreted, cell wall. Note=Stored in
CC the periplasm of gametes until its release. Secreted concurrently with
CC release of the cell walls.
CC -!- INDUCTION: By the signal of flagellar agglutination between gametes of
CC the opposite mating type.
CC -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC dissociation of the cysteine from the zinc ion upon the activation-
CC peptide release activates the enzyme.
CC -!- PTM: Present in 2 forms: an inactive V-form in vegetative cells and an
CC active and soluble G-form. The V-form enzyme may be converted to the G-
CC form enzyme during gametic differentiation under nitrogen-starved
CC conditions.
CC -!- SIMILARITY: Belongs to the peptidase M11 family. {ECO:0000305}.
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DR EMBL; M94265; AAA33094.1; -; mRNA.
DR EMBL; D10542; BAA01400.1; -; mRNA.
DR PIR; A45287; A45287.
DR AlphaFoldDB; P31178; -.
DR STRING; 3055.EDO96296; -.
DR MEROPS; M11.001; -.
DR EnsemblPlants; PNW70408; PNW70408; CHLRE_17g718500v5.
DR Gramene; PNW70408; PNW70408; CHLRE_17g718500v5.
DR BRENDA; 3.4.24.38; 1318.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR021158; Pept_M10A_Zn_BS.
DR InterPro; IPR008752; Peptidase_M11.
DR InterPro; IPR016517; Peptidase_M11_autolysin.
DR Pfam; PF05548; Peptidase_M11; 1.
DR PIRSF; PIRSF007635; Autolysin; 1.
DR PROSITE; PS00546; CYSTEINE_SWITCH; 1.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation; Direct protein sequencing;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Periplasm;
KW Protease; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..183
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:1584806"
FT /id="PRO_0000028870"
FT CHAIN 184..638
FT /note="Autolysin"
FT /id="PRO_0000028871"
FT REGION 269..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 95..102
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 269..285
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 397
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 638 AA; 69833 MW; D3E3467701177251 CRC64;
MSLATRRFGA AAALLVAACV LCTAPAWAQN ETTGTGMVKT KSAFRWIRPP PARPPPFRRP
PPAQTPYVHK VEYTELQILC PQTIDSVTGY PMDDPRCNVP RATVAAGEEA LTIRNEFELL
NGDVLNVTLE EVDTPENPSR RRLLSIIREE QRTGRVLLAT SAELPTPTFR LKSLKSILKG
SQKEIYAGKP IDLRTIVYIM DFSSCKLSGW SAPATLTPEK VTSDMLRGAS APTNNLANYY
GACSYEKTLF NPDNFLVLGP VPVPCIGGVT PPPRPPRPPR PPPRAGSTIS SLSRRNDTYD
DWWDLSKYCT ASEQQAWERA AEAYAQAIVA QDPNSATGKK LQGILQWRER RRNIYILPPG
VKCSWSGYAD VTCTSATCSA YVRGYSDTNA MQVIMHEAMH NYGLEHAGRG TLEYGDATDV
MGDFNKAGKG LLCPNAPNMY RIGWAKPINE PGVAPFQNAT GAWGNLTAAN FTTDPWIRGL
VIPAQGTRDD NMIVVNVGAQ STRDGAMKAT GAQAYYFSYR IKNTTAGGYD SGLTLDFHKK
VLVHAYNGIQ SERVFGFKSN LLDWGPNFQS RSNTWTSPFL AYNNGLGGGV RLVVQSTSDT
QAVVDICRIS ENGKELSCDD GIDNDCDGLQ DNEDPDCQ
