ID   Y1196_STAAS             Reviewed;         428 AA.
AC   Q6G9V1;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Putative zinc metalloprotease SAS1196;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=SAS1196;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX571857; CAG42973.1; -; Genomic_DNA.
DR   RefSeq; WP_000121122.1; NC_002953.3.
DR   AlphaFoldDB; Q6G9V1; -.
DR   SMR; Q6G9V1; -.
DR   KEGG; sas:SAS1196; -.
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..428
FT                   /note="Putative zinc metalloprotease SAS1196"
FT                   /id="PRO_0000088463"
FT   TRANSMEM        172..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        352..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        401..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          186..269
FT                   /note="PDZ"
FT   ACT_SITE        22
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         21
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         25
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   428 AA;  48136 MW;  79242B65662757D2 CRC64;
     MSYLVTIIAF IIVFGVLVTV HEYGHMFFAK RAGIMCPEFA IGMGPKIFSF RKNETLYTIR
     LLPVGGYVRM AGDGLEEPPV EPGMNVKIKL NEENEITHII LDDHHKFQQI EAIEVKKCDF
     KDDLFIEGIT AYDNERHHFK IARKSFFVEN GSLVQIAPRD RQFAHKKPWP KFLTLFAGPL
     FNFILALVLF IGLAYYQGTP TSTVEQVADK YPAQQAGLQK GDKIVQIGKY KISEFDDVDK
     ALDKVKDNKT TVKFERDGKT KSVELTPKKT ERKLTKVSSE TKYVLGFQPA SERTLFKPIV
     YGFESFLKGS TLIFTAVVGM LASIFTGGFS FDMLNGPVGI YHNVDSVVKA GIISLIGYTA
     LLSVNLGIMN LIPIPALDGG RILFVIYEAI FRKPVNKKAE TTIIAIGAIF MVVIMILVTW
     NDIRRYFL