ID A0A0K8P2Z2_IDESA Unreviewed; 680 AA.
AC A0A0K8P2Z2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Dipeptidyl carboxypeptidase Dcp {ECO:0000313|EMBL:GAP37011.1};
DE EC=3.4.15.5 {ECO:0000313|EMBL:GAP37011.1};
GN ORFNames=ISF6_2866 {ECO:0000313|EMBL:GAP37011.1};
OS Ideonella sakaiensis (strain NBRC 110686 / TISTR 2288 / 201-F6).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Piscinibacter.
OX NCBI_TaxID=1547922 {ECO:0000313|EMBL:GAP37011.1, ECO:0000313|Proteomes:UP000037660};
RN [1] {ECO:0000313|Proteomes:UP000037660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110686 / TISTR 2288 / 201-F6
RC {ECO:0000313|Proteomes:UP000037660};
RA Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT "Discovery of a poly(ethylene terephthalate assimilation.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAP37011.1, ECO:0000313|Proteomes:UP000037660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110686 / TISTR 2288 / 201-F6
RC {ECO:0000313|Proteomes:UP000037660};
RX PubMed=26965627; DOI=10.1126/science.aad6359;
RA Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT "A bacterium that degrades and assimilates poly(ethylene terephthalate).";
RL Science 351:1196-1199(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAP37011.1}.
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; BBYR01000041; GAP37011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K8P2Z2; -.
DR STRING; 1547922.ISF6_2866; -.
DR Proteomes; UP000037660; Unassembled WGS sequence.
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; 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:GAP37011.1};
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:UP000037660};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 233..677
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 680 AA; 75476 MW; AFAC4EFDF0C141A3 CRC64;
MDMPTNALLI DWNAPVSLPD FSRIRAEDFR PALERAMALH REELARIASD PRPPGFDDTL
GAYDRAGELL RRTESVFHSL AASATSPELQ AVQREMAGPL AAHASAVLQD EALFRRIDAV
HARRDALGLD AEQRRLVERV HNDFVRAGAA LAPAARARYA EIMQRLAALT TAFGQHVLQA
ESSYALPLPD EAAMAGLPEF VRAAARQAGA ERGLGGPVIT LSRSLIVPFL SFSERRDLRE
AAWRAWVGRG EADGAHDNRP IAAEILALRQ EQARLLGYAT FADYAIADNM AGTRERVWAL
LDEVWARALP AVERERAMLA QAQAAAGASG PIEAWDWRYW AEKVRQQHYA LDEAALKPYF
PLPAMVAAAF DCAQRLFGIR FTPRRELAAY HPDVDVYEVA DAAGRVIGLF LHDNFARATK
RSGAWMNTLS NQHRNGAEQV PVVLNNNNFA KAGAGEPTLL SPDDVRTLFH EFGHGLHGLL
SDVRYQRLAG TEVLRDFVEL PSQLYEHWAQ EREVLRRHAR HWQTGEPLPD ALIERLEAAR
QFGQGYETVR YTASAIVDLA AHEQAEPIDD VVAFEARVMA ERGLPPAVGM NHRLPHFQHL
FAGSGYAAGY YVYLWAEVLD ADAYDAFVEA GDPFDPATAE RLLRCIYARG DSVEPAATYR
AFRGRDPRIE PMLKDRGLLA
//
