ID   Y1262_STAAM             Reviewed;         428 AA.
AC   P63332; Q99UL0;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Putative zinc metalloprotease SAV1262;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=SAV1262;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000017; BAB57424.1; -; Genomic_DNA.
DR   RefSeq; WP_000121119.1; NC_002758.2.
DR   AlphaFoldDB; P63332; -.
DR   SMR; P63332; -.
DR   PaxDb; P63332; -.
DR   EnsemblBacteria; BAB57424; BAB57424; SAV1262.
DR   KEGG; sav:SAV1262; -.
DR   HOGENOM; CLU_025778_1_0_9; -.
DR   OMA; QYMVGFG; -.
DR   PhylomeDB; P63332; -.
DR   BioCyc; SAUR158878:SAV_RS06805-MON; -.
DR   Proteomes; UP000002481; 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 SAV1262"
FT                   /id="PRO_0000088460"
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;  48116 MW;  6158D965663BA5DB 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 SEHTLFKPIV
     YGFESFLKGS TLIFTAVVGM LASIFTGGFS FDMLNGPVGI YHNVDSVVKA GIISLIGYTA
     LLSVNLGIMN LIPIPALDGG RILFVIYEAI FRKPVNKKAE TTIIAIGAIF MVVIMILVTW
     NDIRRYFL