ID   F4LS29_TEPAE            Unreviewed;       375 AA.
AC   F4LS29;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Dipeptidase {ECO:0000313|EMBL:CDI40982.1};
GN   OrderedLocusNames=TEPIRE1_2415 {ECO:0000313|EMBL:CDI40982.1};
OS   Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1).
OC   Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC   Tepidanaerobacteraceae; Tepidanaerobacter.
OX   NCBI_TaxID=1209989 {ECO:0000313|EMBL:CDI40982.1, ECO:0000313|Proteomes:UP000010802};
RN   [1] {ECO:0000313|Proteomes:UP000010802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Re1 {ECO:0000313|Proteomes:UP000010802};
RX   PubMed=23469343; DOI=10.1128/genomeA.00213-12;
RA   Manzoor S., Bongcam-Rudloff E., Schnurer A., Muller B.;
RT   "First genome sequence of a syntrophic acetate-oxidizing bacterium,
RT   Tepidanaerobacter acetatoxydans strain Re1.";
RL   Genome Announc. 1:E00213-E00213(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; HF563609; CDI40982.1; -; Genomic_DNA.
DR   RefSeq; WP_013779287.1; NC_019954.2.
DR   AlphaFoldDB; F4LS29; -.
DR   STRING; 1209989.TepRe1_2247; -.
DR   KEGG; tae:TepiRe1_2415; -.
DR   KEGG; tep:TepRe1_2247; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_031786_0_0_9; -.
DR   OrthoDB; 9761532at2; -.
DR   Proteomes; UP000010802; Chromosome.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 2.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR010964; M20A_pepV-rel.
DR   InterPro; IPR002933; Peptidase_M20.
DR   NCBIfam; TIGR01887; dipeptidaselike; 1.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF33; DIPEPTIDASE SAOUHSC_01868-RELATED; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE   4: Predicted;
KW   Dipeptidase {ECO:0000256|ARBA:ARBA00022997};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022997};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010802};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ   SEQUENCE   375 AA;  42386 MW;  026E58666EF1393B CRC64;
     MEQVLNDKID EYKEKLLKSI IEVVNIPSVK DEPKDNAPFG DRIKEALFVT LDIAENLGFK
     TKNLDNYIGY AQYGDKEEGY IGVIGHLDVV PAGEGWKFPP FSGHIEDEKI YGRGVLDNKG
     PILAALYALY AIKESRLKLS KPVRIIFGTD EESGFNDVRY YLKKEKPPVM GFTPDCKYPV
     VYGERGRANI QFEIEYNDKN YKNAADEFFG FLNDYILSSK SCGDRLGIDF SDAEFGVMEM
     RGHNIHIEDS KFLFNLSLSY PAIVSIDEII KRIKSKLSKN IKLNLLLNYN PVKFDKNSFL
     IKSLQKAYEE VTKLDGTPVT TTGGTYAKIM PNIVPFGPSF PGQKGISHNP NEYMSIEDII
     LNSKIFAQAI YNLAK
//