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Database: UniProt
Entry: T0HRA2_9SPHN
LinkDB: T0HRA2_9SPHN
Original site: T0HRA2_9SPHN 
ID   T0HRA2_9SPHN            Unreviewed;       408 AA.
AC   T0HRA2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, 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=L288_17365 {ECO:0000313|EMBL:EQB01810.1};
OS   Sphingobium quisquiliarum P25.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1329909 {ECO:0000313|EMBL:EQB01810.1, ECO:0000313|Proteomes:UP000015525};
RN   [1] {ECO:0000313|EMBL:EQB01810.1, ECO:0000313|Proteomes:UP000015525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P25 {ECO:0000313|EMBL:EQB01810.1,
RC   ECO:0000313|Proteomes:UP000015525};
RX   PubMed=24029763;
RA   Kumar Singh A., Sangwan N., Sharma A., Gupta V., Khurana J.P., Lal R.;
RT   "Draft Genome Sequence of Sphingobium quisquiliarum Strain P25T, a Novel
RT   Hexachlorocyclohexane (HCH)-Degrading Bacterium Isolated from an HCH
RT   Dumpsite.";
RL   Genome Announc. 1:e00717-13(2013).
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:EQB01810.1}.
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DR   EMBL; ATHO01000150; EQB01810.1; -; Genomic_DNA.
DR   RefSeq; WP_021239513.1; NZ_ATHO01000150.1.
DR   AlphaFoldDB; T0HRA2; -.
DR   PATRIC; fig|1329909.3.peg.3348; -.
DR   Proteomes; UP000015525; 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; IPR001261; ArgE/DapE_CS.
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.
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   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          200..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   408 AA;  42534 MW;  D1506F49F8D1002C CRC64;
     MKGLSSSDRD LLDRAAAFPM LALVQRWATV NSGSRNLDGL AATAAMLADS FAALPGEIRL
     VDADPVDAIA ADGRTEQVPH GRHLHLSVRP DAPVRLLLTG HMDTVFPAGH SFQSIRWIDE
     ERLNGPGVAD MKGGLAVMLA ALQAFETSGE ASRVGYEVVI NSDEEVGSPS SAALIRDSAR
     GKLAALTYEP CLPDGTLAGA RAGSGNFSFI VTGRSAHAGR NPEEGRNALL AAADLALRLK
     AASGPGFTCN PARIDGGSPN NVVPDHAVLR VNFRPRSLEG EQQARAAIAS LAEAVARDHD
     LSIHIHGGFG RPPRPMDARA ASLFAFVRDC GAELGLPVGW RDTGGVCDGN NIAACGVPVV
     DTMGVRGGDI HSDAEYLIVP SLAERAQLSA LALLRMAQGR FSPAGGMV
//
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