ID   CTPAL_STAAB             Reviewed;         496 AA.
AC   Q2YXZ9;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Probable CtpA-like serine protease;
DE            EC=3.4.21.-;
GN   OrderedLocusNames=SAB1275c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI80964.1; -; Genomic_DNA.
DR   RefSeq; WP_000342136.1; NC_007622.1.
DR   AlphaFoldDB; Q2YXZ9; -.
DR   SMR; Q2YXZ9; -.
DR   KEGG; sab:SAB1275c; -.
DR   HOGENOM; CLU_017295_3_0_9; -.
DR   OMA; DPHSSYY; -.
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_0000233188"
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;  55289 MW;  B047D61DC26218F1 CRC64;
     MDDKQHTSSS DDERAEIATS NQDQQTNSSK RVHLKRWQFI SILIGTILIT AVITVVAYIF
     INQKINGLNK TDQANLNKIE NVYKILNSDY YKKQSSDKLS 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 QFDQALENQV KAFQQTNKLE VTGEFNKETN NKFTELLVEK
     ANKHDDVLDK LINILK