CTPAL_STAAC
ID CTPAL_STAAC Reviewed; 496 AA.
AC Q5HG01;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Probable CtpA-like serine protease;
DE EC=3.4.21.-;
GN OrderedLocusNames=SACOL1455;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
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 S41A family. {ECO:0000305}.
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DR EMBL; CP000046; AAW36658.1; -; Genomic_DNA.
DR RefSeq; WP_000342130.1; NC_002951.2.
DR AlphaFoldDB; Q5HG01; -.
DR SMR; Q5HG01; -.
DR EnsemblBacteria; AAW36658; AAW36658; SACOL1455.
DR KEGG; sac:SACOL1455; -.
DR HOGENOM; CLU_017295_3_0_9; -.
DR OMA; DPHSSYY; -.
DR Proteomes; UP000000530; 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_0000233189"
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; 55277 MW; 391FEDC1496A4CD6 CRC64;
MDDKQHTSSS DDERAEIATS NQDQETNSSK RVHLKRWQFI SILIGTILIT AVITVVAYIF
INQKISGLNK TDQSNLNKIE 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 LGYKVDNEST QFDKALENQV KAFQQANKLE VTGEFNKETN NKFTELLVEK
ANKHDDVLDK LINILK