ID   HTRAL_STAAS             Reviewed;         769 AA.
AC   Q6GAJ1;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Serine protease HtrA-like;
DE            EC=3.4.21.-;
GN   OrderedLocusNames=SAS0955;
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR   EMBL; BX571857; CAG42731.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6GAJ1; -.
DR   SMR; Q6GAJ1; -.
DR   KEGG; sas:SAS0955; -.
DR   HOGENOM; CLU_027421_0_0_9; -.
DR   OMA; KRNMAIN; -.
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:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   Pfam; PF13180; PDZ_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Membrane; Protease; Serine protease;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..769
FT                   /note="Serine protease HtrA-like"
FT                   /id="PRO_0000252469"
FT   TRANSMEM        410..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          680..733
FT                   /note="PDZ"
FT   REGION          1..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..204
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..265
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..298
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..332
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..366
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..390
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        504
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        534
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        619
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   769 AA;  86485 MW;  EA34437C8715D278 CRC64;
     MDIGKKHVIP KSQYRRKRRE FFHNEDREEN LNQHQDKQNI DNTTSKKADK QIHKDSIDKH
     ERFKNSLSSH LEQRNRDVNE NKAEESKSNQ DSKSAYNRDH YLTDDVSKKQ NSLDSVDQDT
     EKSKYYEQNS EATLSTKSTD KVESTDMRKL SSDKNKVGHE EQHVLSKPSE HDKETRIDFE
     SSRTDSDSSM QTEKIKKDSS DGNKSSNLKS EVISDKSNTV PKLSESDDEV NNQKPLTLPE
     EQKLKRQQSQ NEQTKTYTYG DSEQNDKSNY ENDLSHHMPS ISDDKDNVMR ENHIVDDNPD
     NDINTPSLSK TDDDRKLDEK IHVEDKHKQN ADSSETVGYQ SQSSASHRIT EKRNNAINDH
     DKLNGQKPNA KTSANNNQKK ATSKLNKGRA TNNNYSDILK KFWMMYWPKL VILMGIIILI
     VILNAIFNNV NKNDRMNDNN DADAQKYTTT MKNANNTVKS VVTVENETSK DSSLPKDKAS
     QDEVGSGVVY KKSGDTLYIV TNAHVVGDKE NQKITFSNNK SVVGKVLGKD KWSDLAVVKA
     TSSDSSVKEI AIGDSNNLVL GEPILVVGNP LGVDFKGTVT EGIISGLNRN VPIDFDKDNK
     YDMLMKAFQI DASVNPGNSG GAVVNREGKL IGVVAAKISM PNVENMSFAI PVNEVQKIVK
     DLETKGKIDY PDVGVKMKNI ASLNSFERQA VKLPGKVKNG VVVDQVDNNG LADQSGLKKG
     DVITELDGKL LEDDLRFRQI IFSHKDDLKS ITAKIYRDGK EKEINIKLK