ID A9BUF0_DELAS Unreviewed; 591 AA.
AC A9BUF0;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Dipeptidase {ECO:0000313|EMBL:ABX33853.1};
GN OrderedLocusNames=Daci_1208 {ECO:0000313|EMBL:ABX33853.1};
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX33853.1, ECO:0000313|Proteomes:UP000000784};
RN [1] {ECO:0000313|EMBL:ABX33853.1, ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT defined pairs of heterotrophic bacteria.";
RL Appl. Environ. Microbiol. 70:4053-4063(2004).
RN [2] {ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000884; ABX33853.1; -; Genomic_DNA.
DR RefSeq; WP_012203139.1; NC_010002.1.
DR AlphaFoldDB; A9BUF0; -.
DR STRING; 398578.Daci_1208; -.
DR GeneID; 24117328; -.
DR KEGG; dac:Daci_1208; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_031786_2_1_4; -.
DR Proteomes; UP000000784; 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; -; 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:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022997};
KW Reference proteome {ECO:0000313|Proteomes:UP000000784};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..591
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002732525"
FT DOMAIN 363..482
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 591 AA; 62783 MW; 01122182BA938102 CRC64;
MKNHPFKAST LALAMSMALA WSGAAGADTL RKPALDALAQ AQPAPTDFAS FLKQAAAAQP
AIAQAVQRHA AGAALTGDEL NHVARLLGLY TRLTQEQAVL ASIERMVALP TVRDPKVPPH
ESPAILAFGE LVQQMARDFG LQYRNVDNRI FEVTLPANTA SASNSGTDEF GILTHADVVP
VVPAEWVLDG QAIDPFKVTR VGDKLYGRGT IDDKGSIATV LFAMKAVKDS GLPLSRGIRL
MIETTEETGG DAMKYYQGKT TLPAYNIVLD SKYPAVVAEK GSGALKAVFD DVKADPAQPA
ITAMAGAASA NAIAQTATAT ITAGDEAAIE AIAARLQAAK GDFTTSYAGQ GGPFTIDIQR
SGTAATVKVT GTSAHGSRPE EGVNPVPRLT LFLQQVLMPT DGVALVQPNA YSNALRYING
AFGLDYFGKQ LGVAYADDFM GPLTLSPNLI KAADGKLEVT TNVRMPRGKT PEQLRTEVEQ
RITRWSAAAK VPLTLQYTQG NWMARDPKGA WLSTLLNIFG DTTGLDAKPV PTAGSTTAKL
MPNAINFGPA MPGKKYTAHN ALEYKELPDL RADMQMFTEM LVRIGNLKQM Q
//
