ID   HTRAL_STAAC             Reviewed;         769 AA.
AC   Q5HH63;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Serine protease HtrA-like;
DE            EC=3.4.21.-;
GN   OrderedLocusNames=SACOL1028;
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   -!- 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; CP000046; AAW36494.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5HH63; -.
DR   SMR; Q5HH63; -.
DR   EnsemblBacteria; AAW36494; AAW36494; SACOL1028.
DR   KEGG; sac:SACOL1028; -.
DR   HOGENOM; CLU_027421_0_0_9; -.
DR   OMA; KRNMAIN; -.
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: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_0000252465"
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..263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..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;  86432 MW;  7948E23EAD17CEBB CRC64;
     MDIGKKHVIP KSQYRRKRRE FFHNEDREEN LNQHQDKQNI DNTTSKKADK QIHKDSIDKH
     ERFKNSLSSH LEQRNRDVNE NKAEESKSNQ DSKSAYNRDH YLTDDVSKKQ NSLDSVDQDT
     EKSKYYEQNS EATLSTKSTD KVESTEMRKL SSDKNKVGHE EQHVLSKPSE HDKETRIDSE
     SSRTDSDSSM QTEKIKKDSS DGNKSSNLKS EVISDKSNTV PKLSESDDEV NNQKPLTLPE
     EQKLKRQQSQ NEQTKTYTYG DSEQNDKSNH ENDLSHHIPS ISDDKDNVMR ENHIVDDNPD
     NDINTPSLSK TDDDRKLDEK IHVEDKHKQN ADSSETVGYQ SQSTASHRST EKRNISINDH
     DKLNGQKTNT 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