ID A0A0A2WXU5_9GAMM Unreviewed; 462 AA.
AC A0A0A2WXU5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Peptidase family M20/M25/M40 {ECO:0000313|EMBL:KGQ17844.1};
GN ORFNames=LF41_1697 {ECO:0000313|EMBL:KGQ17844.1};
OS Lysobacter dokdonensis DS-58.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1300345 {ECO:0000313|EMBL:KGQ17844.1, ECO:0000313|Proteomes:UP000030518};
RN [1] {ECO:0000313|EMBL:KGQ17844.1, ECO:0000313|Proteomes:UP000030518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-58 {ECO:0000313|EMBL:KGQ17844.1,
RC ECO:0000313|Proteomes:UP000030518};
RA Kim J.F., Kwak M.-J.;
RT "Genome sequences of Lysobacter dokdonensis DS-58.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGQ17844.1}.
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DR EMBL; JRKJ01000023; KGQ17844.1; -; Genomic_DNA.
DR RefSeq; WP_036171079.1; NZ_JRKJ01000023.1.
DR AlphaFoldDB; A0A0A2WXU5; -.
DR STRING; 1300345.LF41_1697; -.
DR PATRIC; fig|1300345.3.peg.2761; -.
DR eggNOG; COG0624; Bacteria.
DR OrthoDB; 3665926at2; -.
DR Proteomes; UP000030518; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR Gene3D; 1.10.150.900; -; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF32; CONSERVED PROTEIN; 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.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030518};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..462
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001996523"
FT DOMAIN 213..357
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 462 AA; 49287 MW; 28B5DE55E09421D5 CRC64;
MTRTLLGAML ALTIAAPCAA ADLTPEQARA REIYSTLIAY NTAEGNAQVP VMAKWLAKQF
RDAGFAEADI HVLPVGETAS LVVRYPGDGS GGKPILLMAH MDVVAADPKD WKRDPFKLVE
ENGYFFGRGT SDVKDGIATL TATFLRLKKE GFVPTRDLVI VFTGDEETQM ATTRDLTTTH
RTLIDAEYAL NADGGGGTLE EDGTPRSYSM QTAEKTYADF ELTTHNPGGH SSRPTPRNAI
YELADALKKV QAHAFPVMWN DTTVAELRAE GKVAPGAVGA AMAAFAKDQR DAKAIATLAA
DPGSVGRIRT TCVATMLRGG HGRNALPQSA TANVNCRIFP GTPVDDVRKT LQGVVGQDVE
VTTIGSPVSS DASPLRPDVV AAVTRAVHTL YPGIEIVPNQ SSGATDGMYF RSAGIPTYGV
SGMFAKDSDA FAHGLDERVP VKGFYDGLDY WYVLLKDLAG KK
//