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}.
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; 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
//