ID C7R3Z0_JONDD Unreviewed; 705 AA.
AC C7R3Z0;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Peptidyl-dipeptidase Dcp {ECO:0000313|EMBL:ACV08847.1};
DE EC=3.4.15.5 {ECO:0000313|EMBL:ACV08847.1};
GN OrderedLocusNames=Jden_1191 {ECO:0000313|EMBL:ACV08847.1};
OS Jonesia denitrificans (strain ATCC 14870 / DSM 20603 / BCRC 15368 / CIP
OS 55.134 / JCM 11481 / NBRC 15587 / NCTC 10816 / Prevot 55134) (Listeria
OS denitrificans).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Jonesiaceae;
OC Jonesia.
OX NCBI_TaxID=471856 {ECO:0000313|EMBL:ACV08847.1, ECO:0000313|Proteomes:UP000000628};
RN [1] {ECO:0000313|EMBL:ACV08847.1, ECO:0000313|Proteomes:UP000000628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14870 / DSM 20603 / BCRC 15368 / CIP 55.134 / JCM 11481 /
RC NBRC 15587 / NCTC 10816 / Prevot 55134
RC {ECO:0000313|Proteomes:UP000000628};
RX PubMed=21304666; DOI=10.4056/sigs.41646;
RA Pukall R., Gehrich-Schroter G., Lapidus A., Nolan M., Glavina Del Rio T.,
RA Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F., Copeland A.,
RA Saunders E., Brettin T., Detter J.C., Bruce D., Goodwin L., Pati A.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Goker M.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Han C.;
RT "Complete genome sequence of Jonesia denitrificans type strain (Prevot
RT 55134).";
RL Stand. Genomic Sci. 1:262-269(2009).
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 ---------------------------------------------------------------------------
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; CP001706; ACV08847.1; -; Genomic_DNA.
DR AlphaFoldDB; C7R3Z0; -.
DR STRING; 471856.Jden_1191; -.
DR KEGG; jde:Jden_1191; -.
DR eggNOG; COG0339; Bacteria.
DR HOGENOM; CLU_001805_4_0_11; -.
DR Proteomes; UP000000628; 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:ACV08847.1};
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:UP000000628};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 248..699
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 705 AA; 78722 MW; 0F62ADEF2CF593C1 CRC64;
MGDMSAHIND LDSPFATDSS LPFALPNFAA LTTADYEPAI RAGIAAELAE IDAIVAQNDP
PTVSNTLDAF ETSGQLLSRV MSVFDNELSS NTNEELDDLD ERLAPVLSAH HDDIYLNDAL
YSRLRSLEEI LRHNDATHGT EHHTSADTEA RYLLSTTLRD FVRAGVELSD DKKQQLRTLN
EQASTLESAF GRTLLAGTNA AAILVTNETE LQGVPDDVRA SAAAAARERG HDQGWLLELQ
LPTVQPILAH VASRTLREKI HRASVNRGLG GEHDTRQILL DLVRVRAEIA QLLGYEHWAA
YVAEDSTAGT TPAINDMLTS LVAPAVRNAR REAEVLTQAL RDELHDDTAH LQPWDWTYLS
EKVRARDYQL DDAALRPYLE LHRVVHHGVF AAATRLYGIT FHQRDDLKGY HNDVVVYEVH
NADGSPLGLF LADWYTRDTK RGGAWMNNLV EQSFLLNHHP VVVNNLNITP PPAGQPTLLT
WDEVITLFHE FGHALHGLFA QSHYPSHSGT QVPRDFVEFP SQVNEMWAWD PELLHNYAVH
YHTGEPLPQQ WIDTLIATRQ FNEGFATTEY LAAAILDQAW HQRQPHELPT NPADVEAFEH
AALTAAGIQL DLVPPRYRST YFNHIFAGGY SAGYYSYIWS EVLDADTVQW FHDNGGATRA
NGDHFRTTLL APGGSANCLS TYRTFRGRDA HREPLLTRRG LLDNN
//
