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Database: UniProt
Entry: Q4JTC8_CORJK
LinkDB: Q4JTC8_CORJK
Original site: Q4JTC8_CORJK 
ID   Q4JTC8_CORJK            Unreviewed;       393 AA.
AC   Q4JTC8;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   SubName: Full=Putative subtilisin-like serine protease {ECO:0000313|EMBL:CAI37929.1};
GN   OrderedLocusNames=jk1752 {ECO:0000313|EMBL:CAI37929.1};
OS   Corynebacterium jeikeium (strain K411).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=306537 {ECO:0000313|EMBL:CAI37929.1, ECO:0000313|Proteomes:UP000000545};
RN   [1] {ECO:0000313|EMBL:CAI37929.1, ECO:0000313|Proteomes:UP000000545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K411 {ECO:0000313|EMBL:CAI37929.1,
RC   ECO:0000313|Proteomes:UP000000545};
RX   PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005;
RA   Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA   Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA   Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT   "Complete genome sequence and analysis of the multiresistant nosocomial
RT   pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT   human skin flora.";
RL   J. Bacteriol. 187:4671-4682(2005).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; CR931997; CAI37929.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4JTC8; -.
DR   STRING; 306537.jk1752; -.
DR   KEGG; cjk:jk1752; -.
DR   eggNOG; COG1404; Bacteria.
DR   HOGENOM; CLU_701538_0_0_11; -.
DR   OrthoDB; 9798386at2; -.
DR   Proteomes; UP000000545; Chromosome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00306; Peptidases_S8_S53; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CAI37929.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000545};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT   DOMAIN          77..287
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   393 AA;  40094 MW;  0C28BCE290BD3664 CRC64;
     MIIQDSSPHG NCQEGTVAAP GTVPLPDIDA PSYPALHALS RGRDVDVAVI DTGSAGPGVV
     GDRDFCILHG SVVTSVLRAI APEAKVHSFR HNAVASRAEG TVEDLVRAID RALKARVKVI
     NISMVACEDT AELREAIGRA EKAGVLVVAS TGNTGQCPEG APTFPSSLDP VLAVGAVAPR
     KQELAGGIGT GADANTQKAN SADQGRVPAQ YSAPTHWVDV YAPGGPVEGQ VEVRGKVHTI
     IGSPDPFEGT SFAAPVVSGT AALVWQIVPH LSVQEVRELL TTTATPGASG PGLGKQMLVI
     NPAAAVDKAL DLRDARASDS GVASGGNASD GTADARYELQ TVTTQPHQSE AANYSVPVVL
     SLVLALGIIA TVVCRAFSAD SKPPSGSEAT RAN
//
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