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   16-DEC-2008, entry version 59.
DE   RecName: Full=Autolysin;
DE            EC=3.4.24.38;
DE   AltName: Full=Gametolysin;
DE   AltName: Full=Gamete lytic enzyme;
DE            Short=GLE;
DE   Flags: Precursor;
OS   Chlamydomonas reinhardtii.
OC   Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae;
OC   Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 184-203.
RX   MEDLINE=92262506; PubMed=1584806;
RA   Kinoshita T., Fukuzawa H., Shimada T., Saito T., Matsuda Y.;
RT   "Primary structure and expression of a gamete lytic enzyme in
RT   Chlamydomonas reinhardtii: similarity of functional domains to matrix
RT   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
CC       type gametes during mating as a necessary prelude to cell fusion.
CC       This enzyme acts specifically on the framework proteins (inner
CC       wall) of the cell wall, cleaving several model peptides at
CC       specific sites.
CC   -!- CATALYTIC ACTIVITY: Cleavage of the proline- and hydroxyproline-
CC       rich proteins of the Chlamydomonas cell wall; also cleaves
CC       azocasein, gelatin and Leu-Trp-Met-|-Arg-Phe-Ala.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Periplasm. Secreted, cell wall. Note=Stored
CC       in the periplasm of gametes until its release. Secreted
CC       concurrently with release of the cell walls.
CC   -!- INDUCTION: By the signal of flagellar agglutination between
CC       gametes of the opposite mating type.
CC   -!- DOMAIN: The conserved cysteine present in the cysteine-switch
CC       motif binds the catalytic zinc ion, thus inhibiting the enzyme.
CC       The dissociation of the cysteine from the zinc ion upon the
CC       activation-peptide release activates the enzyme.
CC   -!- PTM: Present in 2 forms: an inactive V-form in vegetative cells
CC       and an active and soluble G-form. The V-form enzyme may be
CC       converted to the G-form enzyme during gametic differentiation
CC       under nitrogen-starved conditions.
CC   -!- SIMILARITY: Belongs to the peptidase M11 family.
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DR   EMBL; M94265; AAA33094.1; -; mRNA.
DR   EMBL; D10542; BAA01400.1; -; mRNA.
DR   PIR; A45287; A45287.
DR   MEROPS; M11.001; -.
DR   PRIDE; P31178; -.
DR   GO; GO:0005618; C:cell wall; IEA:UniProtKB-KW.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-KW.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007047; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR001818; Pept_M10A_M12B.
DR   InterPro; IPR006025; Pept_M_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.
DR   PROSITE; PS00142; ZINC_PROTEASE; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Cell wall; Cell wall biogenesis/degradation;
KW   Direct protein sequencing; Glycoprotein; Hydrolase; Metal-binding;
KW   Metalloprotease; Periplasm; Protease; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL        1     28       Potential.
FT   PROPEP       29    183       Activation peptide.
FT                                /FTId=PRO_0000028870.
FT   CHAIN       184    638       Autolysin.
FT                                /FTId=PRO_0000028871.
FT   MOTIF        95    102       Cysteine switch (By similarity).
FT   COMPBIAS     49     62       Pro-rich.
FT   COMPBIAS    271    283       Pro-rich.
FT   ACT_SITE    397    397       By similarity.
FT   METAL        97     97       Zinc; in inhibited form (By similarity).
FT   METAL       396    396       Zinc; catalytic (By similarity).
FT   METAL       400    400       Zinc; catalytic (By similarity).
FT   METAL       406    406       Zinc; catalytic (By similarity).
FT   CARBOHYD     30     30       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    126    126       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    296    296       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    458    458       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    465    465       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    470    470       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    523    523       N-linked (GlcNAc...) (Potential).
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
//