ID   MEP1_COCP7              Reviewed;         276 AA.
AC   C5P3X6; Q71H76;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Extracellular metalloprotease 1;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=MEP1; ORFNames=CPC735_062670;
OS   Coccidioides posadasii (strain C735) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=222929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 19-33; 75-88 AND
RP   130-141, INDUCTION, SUBCELLULAR LOCATION, AND FUNCTION.
RC   STRAIN=C735;
RX   PubMed=16177346; DOI=10.1128/iai.73.10.6689-6703.2005;
RA   Hung C.Y., Seshan K.R., Yu J.J., Schaller R., Xue J., Basrur V.,
RA   Gardner M.J., Cole G.T.;
RT   "A metalloproteinase of Coccidioides posadasii contributes to evasion of
RT   host detection.";
RL   Infect. Immun. 73:6689-6703(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C735;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
CC   -!- FUNCTION: Secreted metalloproteinase that allows assimilation of
CC       proteinaceous substrates. Pays a pivotal role as a pathogenicity
CC       determinant during infections and contributes to the ability of the
CC       pathogen to persist within the mammalian host. Digests an
CC       immunodominant cell surface antigen (SOWgp) and prevents host
CC       recognition of endospores during the phase of development when these
CC       fungal cells are most vulnerable to phagocytic cell defenses.
CC       {ECO:0000269|PubMed:16177346}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16177346}.
CC   -!- INDUCTION: Peaks of expression occur during the endosporulation stage.
CC       {ECO:0000269|PubMed:16177346}.
CC   -!- SIMILARITY: Belongs to the peptidase M43B family. {ECO:0000305}.
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DR   EMBL; AF500214; AAQ07436.1; -; Genomic_DNA.
DR   EMBL; ACFW01000015; EER28394.1; -; Genomic_DNA.
DR   RefSeq; XP_003070539.1; XM_003070493.1.
DR   AlphaFoldDB; C5P3X6; -.
DR   SMR; C5P3X6; -.
DR   MEROPS; M43.008; -.
DR   EnsemblFungi; EER28394; EER28394; CPC735_062670.
DR   GeneID; 9696034; -.
DR   KEGG; cpw:CPC735_062670; -.
DR   VEuPathDB; FungiDB:CPC735_062670; -.
DR   HOGENOM; CLU_048726_0_0_1; -.
DR   PHI-base; PHI:479; -.
DR   Proteomes; UP000009084; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04275; ZnMc_pappalysin_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR008754; Peptidase_M43.
DR   Pfam; PF05572; Peptidase_M43; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Secreted; Signal; Virulence; Zinc.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:16177346"
FT   CHAIN           19..276
FT                   /note="Extracellular metalloprotease 1"
FT                   /id="PRO_0000407200"
FT   REGION          211..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        192
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         195
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   DISULFID        227..253
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   276 AA;  29593 MW;  FD14BCC1770E22B8 CRC64;
     MRVSVPVLAL AFGSLAAAAP NAGRRTCGSV PPPEFFEASE KVAALEESGA FADLQAPIEV
     ETYFHVVASS RSERDGYISD QMLSDQIRVM NEDYAPHGVH FNLRETTRTI NPSWASDGNE
     IAMKRSLRKG GYAALNVYFL KDLGGALGYC YFPTNAAPGS TTFIRDGCSV LSSSVPGGSG
     APYDLGKTAT HEVGHWMGLF HTFQGGCSGQ GDYVSDTPPQ RSPSSGCPVG RDSCPGGGVD
     PIHNYMDYSV DSCMNQFTRG QGTRMSSMWR QFRAGK