HTRAL_STAEQ
ID HTRAL_STAEQ Reviewed; 585 AA.
AC Q5HQE2;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Serine protease HtrA-like;
DE EC=3.4.21.-;
GN OrderedLocusNames=SERP0611;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
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; CP000029; AAW54044.1; -; Genomic_DNA.
DR RefSeq; WP_001829335.1; NC_002976.3.
DR AlphaFoldDB; Q5HQE2; -.
DR SMR; Q5HQE2; -.
DR STRING; 176279.SERP0611; -.
DR EnsemblBacteria; AAW54044; AAW54044; SERP0611.
DR GeneID; 50019136; -.
DR KEGG; ser:SERP0611; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_027421_0_0_9; -.
DR OMA; ISREWAK; -.
DR OrthoDB; 741829at2; -.
DR Proteomes; UP000000531; 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.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Cell membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW Serine protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..585
FT /note="Serine protease HtrA-like"
FT /id="PRO_0000252471"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 516..575
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 320
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 350
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 435
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
SQ SEQUENCE 585 AA; 66222 MW; 01E3500A1D978321 CRC64;
MDNNKKQVIP RSQYRRKRRE YFHNVEREER IRREKIEKEN QAKREQHQTK VNEERVKDNL
RKARIEKLTQ EEIHQQRDDK SYKQKTLNQN NQMNKSKDDD NKIGEESLHD VRVSSDTSTL
PHQNKSIKDY DDSGNESKQH TKLTSKESML GVNSNHTEQD SRSTQPYSSK HSYSQPKDKD
NDNTQQAQFL KKEDKQRNRA ENIKKVNEFK QLVVAFFKEH WPKMLIIIGI IVLLLILNAI
FTTVNKNDHT NDSAFNGTAK DETTAMKIAE NSVKSVVTVE NDLSNDTTVS DNKNESDNEI
GSGVVYKKVG DSIYIFTNAH VVGDQEKQKV TYGNDKSVTG KVIGKDKWSD LAVVKAKVAD
ENIKPMTMGD SNNIKLAEPI LVIGNPLGTD FKGSVSQGIV SGLNRHVPVD IDKNDNYDAL
MKAFQIDAPV NPGNSGGAVV DRDGRLIGIV SLKIDMHNVE GMAFAIPIND VRKIAKELEH
KGKVNYPNTE IKIKNVGDLD DSERNAINLP AKVNHGVLIG EVKENGLGDK AGLKKGDVIV
ELDGKKIEDN LRYRQVIYSH YDDQKTITAK IYRNGAEKNI KIKLK