ID A0A0B5DC81_9CORY Unreviewed; 670 AA.
AC A0A0B5DC81;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Peptidyl-dipeptidase {ECO:0000313|EMBL:AJE33763.1};
GN ORFNames=B842_09570 {ECO:0000313|EMBL:AJE33763.1};
OS Corynebacterium humireducens NBRC 106098 = DSM 45392.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1223515 {ECO:0000313|EMBL:AJE33763.1, ECO:0000313|Proteomes:UP000031524};
RN [1] {ECO:0000313|EMBL:AJE33763.1, ECO:0000313|Proteomes:UP000031524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MFC-5 {ECO:0000313|Proteomes:UP000031524};
RA Ruckert C., Albersmeier A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium humireducens DSM 45392(T),
RT isolated from a wastewater-fed microbial fuel cell.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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; CP005286; AJE33763.1; -; Genomic_DNA.
DR RefSeq; WP_040086397.1; NZ_CP005286.1.
DR AlphaFoldDB; A0A0B5DC81; -.
DR STRING; 1223515.B842_09570; -.
DR KEGG; chm:B842_09570; -.
DR HOGENOM; CLU_001805_4_0_11; -.
DR OrthoDB; 9773538at2; -.
DR Proteomes; UP000031524; Chromosome.
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 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 228..662
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 670 AA; 74066 MW; 714A182602AAC2CB CRC64;
MTSNPLTAPS TLPYELPDFR AIRLEHAVEA FDTALEEHAA EIAAIVADPA EPTWENTVEA
LETSGALLDR VTSWLFNLQG TDSNDEMDAA VAQIVPRLSA HSDAIYQNEG LYQRLLDAPV
PADPESARLH DLLVRRFTRR GAGLDAAGKA RLAEINQRLS SLSESFGRQL LADTRDLAVL
FDDAADLAGL SESRVASARA AAEEAGQEGW LIPLELPTVQ SDQLVLDSAE SRARLYEASQ
RRGLESNREN LLEQVRLRAE RARLLGYDTH ADYVIAEETA GTAEAARRLL FDLAPAAAAN
ADAERKLAGE LAAADVTAAD WPYWQAKVRE RDFSLDEDEL SAYFPLRQVL VDGVFHSANQ
LYGITVVPRE DLHGYAEGVD VWEVLDHDGA GLGLLLTDYR ARPSKRGGAW MSSFVRQSGL
LDRRPVVVNV MGITHPVDGS EPLLTIDQVT TLFHEFGHAL HGLLSDVRYP TLAGTNVPRD
WVEFPSQINE NWAFEPDIVR NYARHVDTGE VIPRELLDAV VAARQFGQGF ATSEYLAAAI
IDLAWHSLTE EEAGKVTSIS DFEEKALEEA GLVVDELAPR YRSTYFNHIF GGGYSAGYYS
YLWAEALDAD GFDWFRGEED RRAAGERFRE HILSRGASLD YTDAFRRLRG RDKDVTPLLH
RRGLAGVELG
//
