ID A0A1T5DHQ1_9BACT Unreviewed; 451 AA.
AC A0A1T5DHQ1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 02-APR-2025, entry version 24.
DE RecName: Full=Dipeptidase {ECO:0000256|RuleBase:RU364089};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU364089};
GN ORFNames=SAMN03080601_01113 {ECO:0000313|EMBL:SKB71268.1};
OS Alkalitalea saponilacus.
OC Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Marinilabiliales;
OC Marinilabiliaceae; Alkalitalea.
OX NCBI_TaxID=889453 {ECO:0000313|EMBL:SKB71268.1, ECO:0000313|Proteomes:UP000191055};
RN [1] {ECO:0000313|EMBL:SKB71268.1, ECO:0000313|Proteomes:UP000191055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24412 {ECO:0000313|EMBL:SKB71268.1,
RC ECO:0000313|Proteomes:UP000191055};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid;
CC Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869,
CC ChEBI:CHEBI:77460; Evidence={ECO:0000256|RuleBase:RU364089};
CC -!- SIMILARITY: Belongs to the peptidase C69 family.
CC {ECO:0000256|RuleBase:RU364089}.
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; FUYV01000004; SKB71268.1; -; Genomic_DNA.
DR RefSeq; WP_079556879.1; NZ_CP021904.1.
DR AlphaFoldDB; A0A1T5DHQ1; -.
DR STRING; 889453.SAMN03080601_01113; -.
DR KEGG; asx:CDL62_16870; -.
DR OrthoDB; 1109933at2; -.
DR Proteomes; UP000191055; Unassembled WGS sequence.
DR GO; GO:0070004; F:cysteine-type exopeptidase activity; IEA:InterPro.
DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR005322; Peptidase_C69.
DR PANTHER; PTHR12994:SF17; LD30995P; 1.
DR PANTHER; PTHR12994; SECERNIN; 1.
DR Pfam; PF03577; Peptidase_C69; 1.
PE 3: Inferred from homology;
KW Dipeptidase {ECO:0000256|RuleBase:RU364089};
KW Hydrolase {ECO:0000256|RuleBase:RU364089};
KW Protease {ECO:0000256|RuleBase:RU364089};
KW Reference proteome {ECO:0000313|Proteomes:UP000191055}.
SQ SEQUENCE 451 AA; 50857 MW; 38A6E7B4916BC428 CRC64;
MIKKILLILL IITSIPLTGG ELVTVVVTNN ASSDGSVFVA QFNLQNSIDI EEHIFFKRKQ
TSPNSVKEIF SSQTGGKIGE IPEKNGTLQI LANTNEHQLT IIGHRFSAKE ELRNQKGMLD
GENLKRIALQ RSTSAHDAIN TIAALAEKHG YNGNGYRFFI ADPSEVWMME MTGKGAMNRG
AVWVARLIPD GRMAVHGIEP SIGSFPISSR NNDVLYSQDV ISFAREMGFF DGRNRDFNFK
NAYTDPQSND ENSGIVRETA GLFNASIHQR SDSVSLPLFF QPSQKVSLRS VKELTKKLHH
GEETDSVNTD KTVSTFIVQL RNWLPRPIGG VVWLWVGGDS IGNFQPFYIG IDEFPPSFRE
KHDIIGEINR ICANRTDSAI LDECMRIRHE LEEKYLRFAP AVEQTARALF VSNPALAVEY
LTDYCFSQSL IAKRRWREYL EELQNMENIN H
//