ID   F9VH31_LACGL            Unreviewed;       473 AA.
AC   F9VH31;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Dipeptidase {ECO:0000313|EMBL:BAK59664.1};
GN   OrderedLocusNames=LCGL_0204 {ECO:0000313|EMBL:BAK59664.1};
OS   Lactococcus garvieae (strain Lg2) (Enterococcus seriolicida).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=420890 {ECO:0000313|EMBL:BAK59664.1, ECO:0000313|Proteomes:UP000008520};
RN   [1] {ECO:0000313|EMBL:BAK59664.1, ECO:0000313|Proteomes:UP000008520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lg2 {ECO:0000313|EMBL:BAK59664.1,
RC   ECO:0000313|Proteomes:UP000008520};
RX   PubMed=21829716; DOI=10.1371/journal.pone.0023184;
RA   Morita H., Toh H., Oshima K., Yoshizaki M., Kawanishi M., Nakaya K.,
RA   Suzuki T., Miyauchi E., Ishii Y., Tanabe S., Murakami M., Hattori M.;
RT   "Complete genome sequence and comparative analysis of the fish pathogen
RT   Lactococcus garvieae.";
RL   PLoS ONE 6:E23184-E23184(2011).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; AP009333; BAK59664.1; -; Genomic_DNA.
DR   RefSeq; WP_014024205.1; NC_017490.1.
DR   AlphaFoldDB; F9VH31; -.
DR   STRING; 420890.LCGL_0204; -.
DR   KEGG; lgv:LCGL_0204; -.
DR   PATRIC; fig|420890.5.peg.201; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_031786_2_0_9; -.
DR   Proteomes; UP000008520; Chromosome.
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   CDD; cd03888; M20_PepV; 1.
DR   Gene3D; 3.30.70.360; -; 2.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR010964; M20A_pepV-rel.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01887; dipeptidaselike; 1.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF33; DIPEPTIDASE SAOUHSC_01868-RELATED; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Dipeptidase {ECO:0000256|ARBA:ARBA00022997};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022997};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022997};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008520}.
FT   DOMAIN          256..364
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   473 AA;  53119 MW;  C884DD4A9F25DCEE CRC64;
     MTIDFKGEVE KRKEAFLQDL MALLKIKSER KDEEANREFP FGPGPSLAML EFLKIAHKDG
     FKTENFENYV GEVHYGQGEE TLGIFVHADV VPAGQGWTNP PYEPTLREGR LYARGVLDNK
     GPALATYYAL KILKEAGVPF YKKVNFIIGT DEESGWKDMA YYLPKVQLPD FGFSPDARFP
     VVNGEKSNLT EYLHFGPKNA GDFILHDFRS GEQENCVPEE AQALLTSPLD LKIDFEKYLK
     NHKLEGRYAK TGAKTSLQIK GKSAHSSTPE IGKNAATYLA KFLAAYEFGA DAQKFLEVAG
     PKLHKDFEGK SIGIAYEDED MGKLSVNPSV FHFEETGQEN KIALNIRHPK GLTEQDIQER
     LTKHLASFIQ KVSISALINY QPHYLAPEDP LVQVLLSTYR EHTGDDSPPQ TVGGGTYGRL
     MKRGVAYGAL FPDSAFTMHQ TDEHIKLEEL YKAIEIYTDA IYRLVCVKEE KNA
//