CTPAL_STAAS
ID CTPAL_STAAS Reviewed; 496 AA.
AC Q6G9E1;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Probable CtpA-like serine protease;
DE EC=3.4.21.-;
GN OrderedLocusNames=SAS1363;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
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; BX571857; CAG43139.1; -; Genomic_DNA.
DR RefSeq; WP_000342126.1; NC_002953.3.
DR AlphaFoldDB; Q6G9E1; -.
DR SMR; Q6G9E1; -.
DR KEGG; sas:SAS1363; -.
DR HOGENOM; CLU_017295_3_0_9; -.
DR OMA; TFNQVDW; -.
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_0000233193"
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..19
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; 55275 MW; 9A41BE6069218604 CRC64;
MDDKQHTSSS DDERAEIATS NQDQETNSSK RVHLKRWQFI SILIGTILIT AVITVVAYIF
INQKISGLNK TDQANLNKIE NVYKILNSDY YKKQDSDKLS 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 LGYKVDNETT QFDQALENQV KAFQQANKLE VTGEFNKETN NKFTELLVEK
ANKHDDVLDK LINILK