ID Q4JWQ4_CORJK Unreviewed; 712 AA.
AC Q4JWQ4;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Peptidyl-dipeptidase {ECO:0000313|EMBL:CAI36753.1};
DE EC=3.4.15.5 {ECO:0000313|EMBL:CAI36753.1};
GN Name=dcp {ECO:0000313|EMBL:CAI36753.1};
GN OrderedLocusNames=jk0594 {ECO:0000313|EMBL:CAI36753.1};
OS Corynebacterium jeikeium (strain K411).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=306537 {ECO:0000313|EMBL:CAI36753.1, ECO:0000313|Proteomes:UP000000545};
RN [1] {ECO:0000313|EMBL:CAI36753.1, ECO:0000313|Proteomes:UP000000545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K411 {ECO:0000313|EMBL:CAI36753.1,
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR EMBL; CR931997; CAI36753.1; -; Genomic_DNA.
DR RefSeq; WP_005296377.1; NC_007164.1.
DR AlphaFoldDB; Q4JWQ4; -.
DR STRING; 306537.jk0594; -.
DR GeneID; 3433689; -.
DR KEGG; cjk:jk0594; -.
DR PATRIC; fig|306537.10.peg.605; -.
DR eggNOG; COG0339; Bacteria.
DR HOGENOM; CLU_001805_4_0_11; -.
DR OrthoDB; 9773538at2; -.
DR Proteomes; UP000000545; Chromosome.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06456; M3A_DCP; 1.
DR Gene3D; 1.10.1370.40; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR034005; M3A_DCP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:CAI36753.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000000545};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 222..708
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 712 AA; 77731 MW; 840B042ADED1CE4F CRC64;
MDYLQNASEL PYELPDFAAI DLAELVPAFR TALVDHAAQI AAIANNPEAP TWENTAEAWE
ESGQMLQRVL AIVFNYTGAN ATDQVREIEA TISPELARHF SEIWLNRKLW ERICDLPEQP
EGSEEEALLR ELKKSFIRGG AELDDAQRES LRDIDAQLAE LTTAFGAQLQ TATEDAAVLL
TDEAEVAGLS AADKEYFAKA ANERGEEGWL IRLGLPSIQP VLESLENPAA RAKVHEASLN
RAAGSNEATL LQIVRLRAQR AELLGFANHA EFVAAAETAG SLAAVEDLLN QVTPAAVANA
HGEYKRALDK MAVSGTEPSA GTESAAGTAG LSGADWPYWD AQLRAEELDV DEAELKKYFP
LEQVMVDGAF FAAKRLYGID VRERTDLAGY APGVRVWEVT EGEESPVGIG LLLTDMYARP
TKRGGAWMNS FVEQSNLLGK APVVVNVMNI AEPAEGEQAL LTLDEVQTVF HEFGHALHGL
LSDVRYPTLS GTNVPRDFVE FPSQINENWA LEPAVLRNYA RHVETGEVIS GEFVDAIRAQ
AKWGQGLATT EFLAACWLDL AWHKLSAAEA EQLAATDDAA AQVESFEAEA LERAGVDVNG
ALAPRYRSAY FNHIFAGGYS ADYWSYLWAE VLDADGFQAF VDTGAAVGES GTDSNDATAD
LDDDDVRFAG ERFRRIILSR GASIDFEDAF WMFRGQQRSV QPLLDRRGLS QG
//