ID A0A242JZ08_9ENTE Unreviewed; 370 AA.
AC A0A242JZ08;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 18-JUN-2025, entry version 31.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OTP10161.1};
GN ORFNames=A5844_001859 {ECO:0000313|EMBL:OTP10161.1};
OS Candidatus Enterococcus wittei.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1987383 {ECO:0000313|EMBL:OTP10161.1, ECO:0000313|Proteomes:UP000194933};
RN [1] {ECO:0000313|EMBL:OTP10161.1, ECO:0000313|Proteomes:UP000194933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10A9_DIV0425 {ECO:0000313|EMBL:OTP10161.1,
RC ECO:0000313|Proteomes:UP000194933};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genomic Center for Infectious Diseases;
RA Earl A., Manson A., Schwartman J., Gilmore M., Abouelleil A., Cao P.,
RA Chapman S., Cusick C., Shea T., Young S., Neafsey D., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus sp. 10A9_DIV0425.";
RL Submitted (MAY-2017) 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:OTP10161.1}.
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DR EMBL; NGMO01000003; OTP10161.1; -; Genomic_DNA.
DR RefSeq; WP_086284934.1; NZ_NGMO01000003.1.
DR AlphaFoldDB; A0A242JZ08; -.
DR STRING; 1987383.A5844_001859; -.
DR Proteomes; UP000194933; Unassembled WGS sequence.
DR GO; GO:0019213; F:deacetylase activity; IEA:InterPro.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR020043; Deacetylase_Atu3266-like.
DR InterPro; IPR047601; EF_0837-like.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR03583; EF_0837; 1.
DR NCBIfam; NF006689; PRK09237.1; 1.
DR PANTHER; PTHR42717; DIHYDROOROTASE-RELATED; 1.
DR PANTHER; PTHR42717:SF1; IMIDAZOLONEPROPIONASE AND RELATED AMIDOHYDROLASES; 1.
DR Pfam; PF22647; EF_0837-like_N; 1.
DR PIRSF; PIRSF039004; ADE_EF_0837; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR039004-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000194933};
KW Zinc {ECO:0000256|PIRSR:PIRSR039004-1}.
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT SITE 153
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-3"
FT MOD_RES 151
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-2"
SQ SEQUENCE 370 AA; 41119 MW; 75DE6FABF1FA30C8 CRC64;
MYDLVIRNAR FITGETMDIG VTTGKIQLVV PTIEGLGREE LSLKDGQYLS AGWIDDHVHC
FEKMSLYYDY PDRIGVDMGV TTVIDAGSTG AENISDFYEY AKKATTNVFA LVNISKKGII
KQDELADLSK IQLTLIEQKI KEFSDFIIGL KARMSQTVVG KNDITPLQLA KKCQKENQEL
PLMVHIGSAP PQLVDILAVM EKGDVLTHCF NGKGNGILDP VTQEIKPFVK KAKAKGVVFD
IGHGTDSFNF HVAEKALQAG IIADSISTDI YIRNRENGPV YDLATTMEKM HIVGYSWIEI
LEKVTNAPAK HFHLKAKGQV KKGFDADFTI FEIHEQKRVL TDSNGNQRES IQHLKPVSVI
IGGVRHECKL
//
