ID   Y1689_STRPQ             Reviewed;         419 AA.
AC   P0DD33; Q79W78; Q8K5S6;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Putative zinc metalloprotease SPs1691;
DE            EC=3.4.24.-;
GN   Name=eep; OrderedLocusNames=SPs1691;
OS   Streptococcus pyogenes serotype M3 (strain SSI-1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=193567;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSI-1;
RX   PubMed=12799345; DOI=10.1101/gr.1096703;
RA   Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y.,
RA   Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H.,
RA   Hattori M., Hamada S.;
RT   "Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-
RT   scale genomic rearrangement in invasive strains and new insights into phage
RT   evolution.";
RL   Genome Res. 13:1042-1055(2003).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR   EMBL; BA000034; BAC64786.1; -; Genomic_DNA.
DR   RefSeq; WP_011055022.1; NC_004606.1.
DR   AlphaFoldDB; P0DD33; -.
DR   SMR; P0DD33; -.
DR   KEGG; sps:SPs1691; -.
DR   HOGENOM; CLU_025778_1_0_9; -.
DR   OMA; QYMVGFG; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004387; Pept_M50_Zn.
DR   InterPro; IPR008915; Peptidase_M50.
DR   PANTHER; PTHR42837; PTHR42837; 1.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   TIGRFAMs; TIGR00054; TIGR00054; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Protease; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..419
FT                   /note="Putative zinc metalloprotease SPs1691"
FT                   /id="PRO_0000411454"
FT   TRANSMEM        169..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        301..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        392..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          175..274
FT                   /note="PDZ"
FT   ACT_SITE        19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         18
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         22
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   419 AA;  45731 MW;  F1CBD53B3F37D6CF CRC64;
     MLGIITFIII FGILVIVHEF GHFYFAKKSG ILVREFAIGM GPKIFSHVDQ GGTLYTLRML
     PLGGYVRMAG WGDDKTEIKT GTPASLTLNE QGFVKRINLS QSKLDPTSLP MHVTGYDLED
     QLSITGLVLE ETKTYKVAHD ATIVEEDGTE IRIAPLDVQY QNASIGGRLI TNFAGPMNNF
     ILGIVVFILL VFLQGGMPDF SSNHVRVQEN GAAAKAGLRD NDQIVAINGY KVNSWNDLTE
     AVNLATRDLG PSQTIKVTYK SHQRLKTVAV KPQKHAKTYT IGVKASLKTG FKDKLLGGLE
     LAWSGAFTIL NALKGLITGF SLNKLGGPVA MYDMSNQAAQ NGLESVLSLM AMLSINLGIF
     NLIPIPALDG GKILMNIIEA IRRKPIKQET EAYITLAGVA IMVVLMIAVT WNDIMRVFF