ID   HTRAL_STAHJ             Reviewed;         639 AA.
AC   Q4L530;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Serine protease HtrA-like;
DE            EC=3.4.21.-;
GN   OrderedLocusNames=SH1936;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(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; AP006716; BAE05245.1; -; Genomic_DNA.
DR   RefSeq; WP_011276206.1; NC_007168.1.
DR   AlphaFoldDB; Q4L530; -.
DR   SMR; Q4L530; -.
DR   STRING; 279808.SH1936; -.
DR   PRIDE; Q4L530; -.
DR   EnsemblBacteria; BAE05245; BAE05245; SH1936.
DR   GeneID; 58061950; -.
DR   KEGG; sha:SH1936; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_027421_0_0_9; -.
DR   OMA; KRNMAIN; -.
DR   OrthoDB; 741829at2; -.
DR   Proteomes; UP000000543; 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..639
FT                   /note="Serine protease HtrA-like"
FT                   /id="PRO_0000252473"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          527..629
FT                   /note="PDZ"
FT   REGION          1..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..94
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..209
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..262
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        374
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        404
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        489
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   639 AA;  72998 MW;  4032662BD9505D22 CRC64;
     MDNDKKHVIP REQYRRKRHE YFHNEEREER LEREREQRER LAKKEQEQAK VNEERVKDNM
     RKARIEKLTQ EEIHQQQHLA KLRSDNESDQ ELNDTNTHHL TLPEEQQLKN EHKENNDKVT
     KPTDEMEKQE KEDNNSASSK HDEIEPKYSR VEKNKGKQKQ DNINKSEVNH LDKSEQTKKH
     KETKESSEDV LETNKSQKIE QKEQKASSNE TSNKELNSYT KDKNNKVEDN QDLKKASSQN
     LAHSNKLEEN EHLENEPKNN DTMDKVKDFL KLHWLKIVIV VAIILIVILI SAIISTMNQN
     SSIEQSSNND TKYTTTMKNA ETAVKSVVTI ENDTPKNITT QTIDKTNINS NNEVGSGVVY
     KAVDDTFFIL TNTHIVGSNK RVNITYDDDK TATATVVGRD MWSDIAVLKA TIKNKNMQPI
     KIGHSKHLKL GESILVVGNP LGNDFKNTVT KGIISGLNRA VPVDFDKDNK NDEWVNTFQI
     DASVNPGNSG GAVVNRVGEL VGLVSLKINM PNIEGMGFAI PIDAAREIAE ELEKKGEIQY
     PNTGIGIKNV SDLMPYERNL LKVPEDVQNG IVVEKLKENG LGKKSGLKIG DVVVELDSKS
     IQNNLQYRQI IFNHRQDLKT LSAKIYREGK SQEIRIKLK