ID   Y1238_STAAR             Reviewed;         428 AA.
AC   Q6GHH3;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Putative zinc metalloprotease SAR1238;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=SAR1238;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
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}.
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DR   EMBL; BX571856; CAG40240.1; -; Genomic_DNA.
DR   RefSeq; WP_000121112.1; NC_002952.2.
DR   AlphaFoldDB; Q6GHH3; -.
DR   SMR; Q6GHH3; -.
DR   KEGG; sar:SAR1238; -.
DR   HOGENOM; CLU_025778_1_0_9; -.
DR   OMA; QYMVGFG; -.
DR   OrthoDB; 1395197at2; -.
DR   Proteomes; UP000000596; 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; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..428
FT                   /note="Putative zinc metalloprotease SAR1238"
FT                   /id="PRO_0000088462"
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;  48137 MW;  651AC0A03FE2AF6B CRC64;
     MSYLVTIIAF IIVFGVLVTV HEYGHMFFAK RAGIMCPEFA IGMGPKIFSF RKNETLYTIR
     LLPVGGYVRM AGDGLEEPPV EPGMNVKIKL NEENEITHII LDDHHKFQQI EAIEVKKCDF
     KDDLFIEGIT AYDNERHHFK IARKSFFVEN GSLVQIAPRD RQFAHKKPWP KFLTLFAGPL
     FNFILALVLF IGLAYYQGTP TSTVEQVADK YPAQQAGIQK GDKIVQIGKY KISEFDDVDK
     ALDKVKDNKT TVKFERDGKT KSVELTPKKT ERKLTKVSSE TKYVLGFQPA SEHTLFKPIV
     YGFKSFLIGS TYIFSAVVGM LASIFTGGFS FDMLNGPVGI YHNVDSVVKA GIISLIGYTA
     LLSVNLGIMN LIPIPALDGG RILFVIYEAI FRKPVNKKAE TTIIAIGAIF MVVIMILVTW
     NDIRRYFL