ID   Y1963_STRP1             Reviewed;         419 AA.
AC   Q99XY3; Q48WI3;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Putative zinc metalloprotease SPy_1963/M5005_Spy1674;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=SPy_1963, M5005_Spy1674;
OS   Streptococcus pyogenes serotype M1.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX   PubMed=11296296; DOI=10.1073/pnas.071559398;
RA   Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA   Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA   Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA   Clifton S.W., Roe B.A., McLaughlin R.E.;
RT   "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX   PubMed=16088826; DOI=10.1086/432514;
RA   Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA   Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA   Musser J.M.;
RT   "Evolutionary origin and emergence of a highly successful clone of serotype
RT   M1 group A Streptococcus involved multiple horizontal gene transfer
RT   events.";
RL   J. Infect. Dis. 192:771-782(2005).
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; AE004092; AAK34656.1; -; Genomic_DNA.
DR   EMBL; CP000017; AAZ52292.1; -; Genomic_DNA.
DR   RefSeq; NP_269935.1; NC_002737.2.
DR   AlphaFoldDB; Q99XY3; -.
DR   SMR; Q99XY3; -.
DR   STRING; 1314.HKU360_01791; -.
DR   PaxDb; Q99XY3; -.
DR   EnsemblBacteria; AAK34656; AAK34656; SPy_1963.
DR   KEGG; spy:SPy_1963; -.
DR   KEGG; spz:M5005_Spy1674; -.
DR   PATRIC; fig|160490.10.peg.1710; -.
DR   HOGENOM; CLU_025778_1_0_9; -.
DR   OMA; QYMVGFG; -.
DR   Proteomes; UP000000750; Chromosome.
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; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..419
FT                   /note="Putative zinc metalloprotease
FT                   SPy_1963/M5005_Spy1674"
FT                   /id="PRO_0000088468"
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"
FT   CONFLICT        84
FT                   /note="A -> T (in Ref. 2; AAZ52292)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   419 AA;  45819 MW;  B3655F618779548E CRC64;
     MLGIITFIII FGILVIVHEF GHFYFAKKSG ILVREFAIGM GPKIFSHVDQ GGTLYTLRML
     PLGGYVRMAG WGDDKTEIKT GTPASLTLNE QGFVKRINLS QSKLDPTSLP MHVTGYDLED
     QLSITGLVLE ETKTYKVAHD ATIVEEDGTE IRIAPLDVQY QNASIGGRLI TNFAGPMNNF
     ILGIVVFILL VFLQGGMPDF SSNHVRVQEN GAAAKAGLRD NDQIVAINGY KVTSWNDLTE
     AVDLATRDLG PSQTIKVTYK SHQRLKTVAV KPQKHAKTYT IGVKASLKTG FKDKLLGGLE
     LAWSRAFTIL NALKGLITGF SLNKLGGPVA MYDMSNQAAQ NGLESVLSLM AMLSINLGIF
     NLIPIPALDG GKILMNIIEA IRRKPIKQET EAYITLAGVA IMVVLMIAVT WNDIMRVFF