ID HTRAL_STAA3 Reviewed; 769 AA.
AC Q2FI55;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Serine protease HtrA-like;
DE EC=3.4.21.-;
GN OrderedLocusNames=SAUSA300_0923;
OS Staphylococcus aureus (strain USA300).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=367830;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USA300;
RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA Perdreau-Remington F.;
RT "Complete genome sequence of USA300, an epidemic clone of community-
RT acquired meticillin-resistant Staphylococcus aureus.";
RL Lancet 367:731-739(2006).
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; CP000255; ABD20429.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2FI55; -.
DR SMR; Q2FI55; -.
DR KEGG; saa:SAUSA300_0923; -.
DR HOGENOM; CLU_027421_0_0_9; -.
DR OMA; KRNMAIN; -.
DR Proteomes; UP000001939; Chromosome.
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 CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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 PANTHER; PTHR43019; SERINE ENDOPROTEASE DEGS; 1.
DR PANTHER; PTHR43019:SF62; SERINE ENDOPROTEASE DEGS; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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_0000252462"
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..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..140
FT /note="Polar 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; 86402 MW; AC900873B7A8C855 CRC64;
MDIGKKHVIP KSQYRRKRRE FFHNEDREEN LNQHQDKQNI DNTTSKKADK QIHKDSIDKH
ERFKNSLSSH LEQRNRDVNE NKAEESKSNQ DSKSAYNRDH YLTDDVSKKQ NSLDSVDQDT
VKSKYYEQNS 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
//
