ID D2QAT5_BIFDB Unreviewed; 455 AA.
AC D2QAT5;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE SubName: Full=Peptidase family M20A protein {ECO:0000313|EMBL:ADB09921.1};
DE EC=3.4.13.20 {ECO:0000313|EMBL:ADB09921.1};
GN OrderedLocusNames=BDP_1303 {ECO:0000313|EMBL:ADB09921.1};
OS Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 / Bd1).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=401473 {ECO:0000313|EMBL:ADB09921.1, ECO:0000313|Proteomes:UP000008693};
RN [1] {ECO:0000313|EMBL:ADB09921.1, ECO:0000313|Proteomes:UP000008693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27534 / DSM 20436 / JCM 1195 / Bd1
RC {ECO:0000313|Proteomes:UP000008693};
RX PubMed=20041198; DOI=10.1371/journal.pgen.1000785;
RA Ventura M., Turroni F., Zomer A., Foroni E., Giubellini V., Bottacini F.,
RA Canchaya C., Claesson M.J., He F., Mantzourani M., Mulas L., Ferrarini A.,
RA Gao B., Delledonne M., Henrissat B., Coutinho P., Oggioni M., Gupta R.S.,
RA Zhang Z., Beighton D., Fitzgerald G.F., O'Toole P.W., van Sinderen D.;
RT "The Bifidobacterium dentium Bd1 genome sequence reflects its genetic
RT adaptation to the human oral cavity.";
RL PLoS Genet. 5:E1000785-E1000785(2009).
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; CP001750; ADB09921.1; -; Genomic_DNA.
DR RefSeq; WP_003839867.1; NC_013714.1.
DR AlphaFoldDB; D2QAT5; -.
DR STRING; 401473.BDP_1303; -.
DR GeneID; 69536534; -.
DR KEGG; bde:BDP_1303; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_029469_2_0_11; -.
DR OMA; HITIPGF; -.
DR Proteomes; UP000008693; Chromosome.
DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43270; BETA-ALA-HIS DIPEPTIDASE; 1.
DR PANTHER; PTHR43270:SF12; SUCCINYL-DIAMINOPIMELATE DESUCCINYLASE; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Dipeptidase {ECO:0000313|EMBL:ADB09921.1};
KW Hydrolase {ECO:0000313|EMBL:ADB09921.1};
KW Protease {ECO:0000313|EMBL:ADB09921.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008693}.
FT DOMAIN 209..351
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 455 AA; 48867 MW; F0D1A3AB2B7B278A CRC64;
MAALLADDIR ARVEGDWDRI VDVLNRKIAL QSISAKGITA EHMRRSAEFV AEELRKVGVD
AKVVQSHNPD GTPGAWEVIG SKIVDEHAPT VLLYAHHDVQ PVPDEGAWDT DPFVGTQIGT
RLYGRGAADD GGGIAIHSGA LKALGDDLKV NVKVFIEGEE EMGSPSFIPF IEEHRDEFRS
DVIIVADSGN WSAEIPSLTT SLRGNTDIDV HVKALEHPVH SGQYGGPILD ANTLAAMLIA
SMYDEHGDLA VPGVAAEEPI GGLQRDLDET TVRADAGIVD SYRLAGTGSL AARLWTKPSV
TVIGFDAHPV EGSFNVISPE TTFRLSLRTA PNQRPQEAQE ALAEFMVEHA PFGAEVWVDR
LDNGMGWAMD PDAEATKDAM EAMEQAFGVA PVNKGEGGSI PFIPELQRIF PNAQVLVTGP
EDPKANAHSP NESISLPGLK NNVITEALLL DKLSR
//