ID   Y1281_STAAC             Reviewed;         428 AA.
AC   Q5HGG9;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Putative zinc metalloprotease SACOL1281;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=SACOL1281;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(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; CP000046; AAW38112.1; -; Genomic_DNA.
DR   RefSeq; WP_000121116.1; NC_002951.2.
DR   AlphaFoldDB; Q5HGG9; -.
DR   SMR; Q5HGG9; -.
DR   EnsemblBacteria; AAW38112; AAW38112; SACOL1281.
DR   KEGG; sac:SACOL1281; -.
DR   HOGENOM; CLU_025778_1_0_9; -.
DR   OMA; QYMVGFG; -.
DR   Proteomes; UP000000530; 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 SACOL1281"
FT                   /id="PRO_0000088459"
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;  48107 MW;  771A400705407C77 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 EKKLTKVSSE TKYVLGFQPA SEHTLFKPIV
     FGFKSFLIGS TYIFTAVVGM LASIFTGGFS FDMLNGPVGI YHNVDSVVKA GIISLIGYTA
     LLSVNLGIMN LIPIPALDGG RILFVIYEAI FRKPVNKKAE TTIIAIGAIF MVVIMILVTW
     NDIRRYFL