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Database: UniProt
Entry: A0A0Q4FRJ1_9SPHN
LinkDB: A0A0Q4FRJ1_9SPHN
Original site: A0A0Q4FRJ1_9SPHN 
ID   A0A0Q4FRJ1_9SPHN        Unreviewed;       402 AA.
AC   A0A0Q4FRJ1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN   ORFNames=ASE75_08150 {ECO:0000313|EMBL:KQM65017.1};
OS   Sphingomonas sp. Leaf17.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1735683 {ECO:0000313|EMBL:KQM65017.1, ECO:0000313|Proteomes:UP000051777};
RN   [1] {ECO:0000313|EMBL:KQM65017.1, ECO:0000313|Proteomes:UP000051777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf17 {ECO:0000313|EMBL:KQM65017.1,
RC   ECO:0000313|Proteomes:UP000051777};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQM65017.1, ECO:0000313|Proteomes:UP000051777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf17 {ECO:0000313|EMBL:KQM65017.1,
RC   ECO:0000313|Proteomes:UP000051777};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQM65017.1}.
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DR   EMBL; LMKL01000005; KQM65017.1; -; Genomic_DNA.
DR   RefSeq; WP_055931748.1; NZ_LMKL01000005.1.
DR   AlphaFoldDB; A0A0Q4FRJ1; -.
DR   STRING; 1735683.ASE75_08150; -.
DR   OrthoDB; 9776600at2; -.
DR   Proteomes; UP000051777; 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   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR017150; Pept_M20_glutamate_carboxypep.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF9; BLL0789 PROTEIN; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF037238; Carboxypeptidase_G2; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051777}.
FT   DOMAIN          201..298
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   ACT_SITE        103
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
FT   ACT_SITE        164
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
SQ   SEQUENCE   402 AA;  41395 MW;  023CB1EDCA1B034D CRC64;
     MRGLSTTERD AVARAGDAPM LQQVLDWAAI NSGTRHLAGV ARMADVLADA FAVLPGRIAL
     VAPDPVDSVD GDGRVGALDH GRHLHLAVRP DAPVQMLFTG HMDTVYPVDH PFQSLTMRDD
     GTLNGPGVAD MKSGLSLMLA ALSAVEASPL ASRIGYEVVI NSDEETGSLS SAALLARAAR
     GKVAALTYEP ALPDGTLAGA RGGTGNFSIT VRGRAAHAGR NPEDGRNAIV AASDLALRLH
     QCRGPRLAVN PARIDGGGPN NVVPDLAVLR VNFRPAGLDD ITRAKSEIDA AVAAVAAAHD
     VHIAVHGGFN RPPKPVDATA ERLLTLVQQA GAALDIPVSW RATGGVCDGN NIAAAGVPVV
     DTMGARGGAI HSTEEFLIVE SLAERAALSA VTILRIAERG GL
//
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