ID   CTPAL_STAAR             Reviewed;         496 AA.
AC   Q6GGY8;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Probable CtpA-like serine protease;
DE            EC=3.4.21.-;
GN   OrderedLocusNames=SAR1432;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
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 S41A family. {ECO:0000305}.
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DR   EMBL; BX571856; CAG40429.1; -; Genomic_DNA.
DR   RefSeq; WP_000342154.1; NC_002952.2.
DR   AlphaFoldDB; Q6GGY8; -.
DR   SMR; Q6GGY8; -.
DR   KEGG; sar:SAR1432; -.
DR   HOGENOM; CLU_017295_3_0_9; -.
DR   OMA; TFNQVDW; -.
DR   OrthoDB; 1646508at2; -.
DR   Proteomes; UP000000596; 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:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07560; Peptidase_S41_CPP; 1.
DR   Gene3D; 1.10.101.10; -; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004447; Peptidase_S41A.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
DR   InterPro; IPR005151; Tail-specific_protease.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF03572; Peptidase_S41; 1.
DR   Pfam; PF01471; PG_binding_1; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00245; TSPc; 1.
DR   SUPFAM; SSF47090; SSF47090; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR00225; prc; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Membrane; Protease; Serine protease;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..496
FT                   /note="Probable CtpA-like serine protease"
FT                   /id="PRO_0000233192"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          124..206
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        329
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        340
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        354
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   496 AA;  55259 MW;  D7503B15F3EA58DB CRC64;
     MDDKQHTTSS DDERAENATS NQDQQTNSSK RVHLKRWQFI SILIGTIIIT AVITVVAYIF
     INQKISGLNK TDQANLNKIE NVYKILNSDY YKKQNSDKLS KAAIDGMVKE LKDPYSEYLT
     KEQTKSFNEG VSGDFVGIGA EMQKKNDQIM VTSPMKGSPA ERAGIRPKDV ITKVNGKSIK
     GKALDEVVKD VRGKENTEVT LTVQRGSEEK DVKIKREKIH VKSVEYKKKG KVGVITINKF
     QNDTSGELKD AVLKAHKDGL KKIVLDLRNN PGGLLDEAVK MANIFIDKGK TVVKLEKGKD
     TEAIQTSNDA LKEAKDMDIS ILVNEGSASA SEVFTGALKD YNKAKVYGSK TFGKGVVQTT
     REFKDGSLLK YTEMKWLTPD GHYIHGKGIK PDVTIDTPKY QSLNVIPNTK TFKVGDDDKN
     IKTIKIGLSA LGYKVDNEST QFDQALENLV KAFQQANKLE VTGEFNKETN NKFTELLVEK
     ANKHDDVLDK LINILK