PEPV_LACDL
ID PEPV_LACDL Reviewed; 470 AA.
AC P45494;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Beta-Ala-Xaa dipeptidase;
DE EC=3.4.13.-;
DE AltName: Full=Beta-Ala-His dipeptidase;
DE AltName: Full=Peptidase V;
GN Name=pepV;
OS Lactobacillus delbrueckii subsp. lactis.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=29397;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBSTRATE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RC STRAIN=DSM 7290 / WS87;
RX PubMed=7528082; DOI=10.1099/00221287-140-10-2591;
RA Vongerichten K.F., Klein J.R., Matern H., Plapp R.;
RT "Cloning and nucleotide sequence analysis of pepV, a carnosinase gene from
RT Lactobacillus delbrueckii subsp. lactis DSM 7290, and partial
RT characterization of the enzyme.";
RL Microbiology 140:2591-2600(1994).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND
RP ZINC, AND COFACTOR.
RX PubMed=12176387; DOI=10.1016/s0969-2126(02)00805-5;
RA Jozic D., Bourenkow G., Bartunik H., Scholze H., Dive V., Henrich B.,
RA Huber R., Bode W., Maskos K.;
RT "Crystal structure of the dinuclear zinc aminopeptidase PepV from
RT Lactobacillus delbrueckii unravels its preference for dipeptides.";
RL Structure 10:1097-1106(2002).
CC -!- FUNCTION: Is a relatively unspecific dipeptidase cleaving a variety of
CC dipeptides, notably those with an N-terminal beta-Ala or D-Ala residue,
CC e.g. carnosine (beta-Ala-His). To a lesser extent, also shows
CC aminopeptidase activity, since it is able to catalyze the removal of
CC the N-terminal amino acid from a few distinct tripeptides.
CC {ECO:0000269|PubMed:7528082}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:12176387};
CC Note=Binds 2 Zn(2+) ions per subunit. These two catalytic ions are both
CC involved in the stabilization of the tetrahedral intermediate and in
CC the activation of the catalytic water molecule.
CC {ECO:0000269|PubMed:12176387};
CC -!- ACTIVITY REGULATION: Fully inhibited by 1,10-phenanthroline or EDTA.
CC {ECO:0000269|PubMed:7528082}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:7528082}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR EMBL; Z31377; CAA83252.1; -; Genomic_DNA.
DR PIR; S57902; S57902.
DR PDB; 1LFW; X-ray; 1.80 A; A=1-470.
DR PDBsum; 1LFW; -.
DR AlphaFoldDB; P45494; -.
DR SMR; P45494; -.
DR DrugBank; DB03340; 3-[(1-Amino-2-Carboxy-Ethyl)-Hydroxy-Phosphinoyl]-2-Methyl-Propionic Acid.
DR MEROPS; M20.004; -.
DR EvolutionaryTrace; P45494; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR010964; M20A_pepV-rel.
DR InterPro; IPR011291; Pept_M20A_peptidaseV.
DR InterPro; IPR002933; Peptidase_M20.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01886; dipeptidase; 1.
DR TIGRFAMs; TIGR01887; dipeptidaselike; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Dipeptidase; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Zinc.
FT CHAIN 1..470
FT /note="Beta-Ala-Xaa dipeptidase"
FT /id="PRO_0000185276"
FT ACT_SITE 89
FT /evidence="ECO:0000250"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12176387"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12176387"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12176387"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12176387"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12176387"
FT BINDING 350
FT /ligand="substrate"
FT BINDING 439
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12176387"
FT HELIX 5..10
FT /evidence="ECO:0007829|PDB:1LFW"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:1LFW"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:1LFW"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1LFW"
FT HELIX 43..58
FT /evidence="ECO:0007829|PDB:1LFW"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:1LFW"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:1LFW"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:1LFW"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:1LFW"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:1LFW"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:1LFW"
FT HELIX 121..137
FT /evidence="ECO:0007829|PDB:1LFW"
FT STRAND 142..151
FT /evidence="ECO:0007829|PDB:1LFW"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:1LFW"
FT HELIX 158..166
FT /evidence="ECO:0007829|PDB:1LFW"
FT STRAND 171..186
FT /evidence="ECO:0007829|PDB:1LFW"
FT STRAND 188..196
FT /evidence="ECO:0007829|PDB:1LFW"
FT STRAND 204..212
FT /evidence="ECO:0007829|PDB:1LFW"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:1LFW"
FT HELIX 232..246
FT /evidence="ECO:0007829|PDB:1LFW"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:1LFW"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:1LFW"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:1LFW"
FT HELIX 279..287
FT /evidence="ECO:0007829|PDB:1LFW"
FT HELIX 294..305
FT /evidence="ECO:0007829|PDB:1LFW"
FT TURN 306..309
FT /evidence="ECO:0007829|PDB:1LFW"
FT TURN 314..317
FT /evidence="ECO:0007829|PDB:1LFW"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:1LFW"
FT STRAND 329..338
FT /evidence="ECO:0007829|PDB:1LFW"
FT STRAND 343..351
FT /evidence="ECO:0007829|PDB:1LFW"
FT HELIX 357..368
FT /evidence="ECO:0007829|PDB:1LFW"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:1LFW"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:1LFW"
FT HELIX 390..403
FT /evidence="ECO:0007829|PDB:1LFW"
FT STRAND 409..414
FT /evidence="ECO:0007829|PDB:1LFW"
FT HELIX 417..420
FT /evidence="ECO:0007829|PDB:1LFW"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:1LFW"
FT HELIX 447..465
FT /evidence="ECO:0007829|PDB:1LFW"
SQ SEQUENCE 470 AA; 51990 MW; 488117B4F33E4AB0 CRC64;
MDLNFKELAE AKKDAILKDL EELIAIDSSE DLENATEEYP VGKGPVDAMT KFLSFAKRDG
FDTENFANYA GRVNFGAGDK RLGIIGHMDV VPAGEGWTRD PFKMEIDEEG RIYGRGSADD
KGPSLTAYYG MLLLKEAGFK PKKKIDFVLG TNEETNWVGI DYYLKHEPTP DIVFSPDAEY
PIINGEQGIF TLEFSFKNDD TKGDYVLDKF KAGIATNVTP QVTRATISGP DLEAVKLAYE
SFLADKELDG SFEINDESAD IVLIGQGAHA SAPQVGKNSA TFLALFLDQY AFAGRDKNFL
HFLAEVEHED FYGKKLGIFH HDDLMGDLAS SPSMFDYEHA GKASLLNNVR YPQGTDPDTM
IKQVLDKFSG ILDVTYNGFE EPHYVPGSDP MVQTLLKVYE KQTGKPGHEV VIGGGTYGRL
FERGVAFGAQ PENGPMVMHA ANEFMMLDDL ILSIAIYAEA IYELTKDEEL
