CTPAL_STAAW
ID CTPAL_STAAW Reviewed; 496 AA.
AC Q8NWR2;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Probable CtpA-like serine protease;
DE EC=3.4.21.-;
GN OrderedLocusNames=MW1310;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S41A family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000033; BAB95175.1; -; Genomic_DNA.
DR RefSeq; WP_000342126.1; NC_003923.1.
DR AlphaFoldDB; Q8NWR2; -.
DR SMR; Q8NWR2; -.
DR EnsemblBacteria; BAB95175; BAB95175; BAB95175.
DR KEGG; sam:MW1310; -.
DR HOGENOM; CLU_017295_3_0_9; -.
DR OMA; TFNQVDW; -.
DR Proteomes; UP000000418; 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_0000233194"
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