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Database: UniProt
Entry: A0A069RF82_PEPLI
LinkDB: A0A069RF82_PEPLI
Original site: A0A069RF82_PEPLI 
ID   A0A069RF82_PEPLI        Unreviewed;       252 AA.
AC   A0A069RF82;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Putative phosphatase {ECO:0000313|EMBL:KDR95656.1};
DE            EC=3.1.3.- {ECO:0000313|EMBL:KDR95656.1};
GN   ORFNames=CLIT_10c03830 {ECO:0000313|EMBL:KDR95656.1};
OS   Peptoclostridium litorale DSM 5388.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptoclostridium.
OX   NCBI_TaxID=1121324 {ECO:0000313|EMBL:KDR95656.1, ECO:0000313|Proteomes:UP000027946};
RN   [1] {ECO:0000313|EMBL:KDR95656.1, ECO:0000313|Proteomes:UP000027946}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W6 {ECO:0000313|EMBL:KDR95656.1,
RC   ECO:0000313|Proteomes:UP000027946};
RA   Poehlein A., Jagirdar A., Khonsari B., Chibani C.M.,
RA   Gutierrez Gutierrez D.A., Davydova E., Alghaithi H.S., Nair K.P.,
RA   Dhamotharan K., Chandran L., G W., Daniel R.;
RT   "Genome sequence of Clostridium litorale W6, DSM 5388.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01561};
CC       Note=Binds 3 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01561};
CC   -!- SIMILARITY: Belongs to the PHP family. {ECO:0000256|HAMAP-
CC       Rule:MF_01561}.
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:KDR95656.1}.
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DR   EMBL; JJMM01000010; KDR95656.1; -; Genomic_DNA.
DR   RefSeq; WP_038264062.1; NZ_JJMM01000010.1.
DR   AlphaFoldDB; A0A069RF82; -.
DR   STRING; 1121324.CLIT_10c03830; -.
DR   eggNOG; COG1387; Bacteria.
DR   OrthoDB; 9808747at2; -.
DR   Proteomes; UP000027946; Unassembled WGS sequence.
DR   GO; GO:0016791; F:phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   CDD; cd07437; PHP_HisPPase_Ycdx_like; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   HAMAP; MF_01561; YcdX_phosphat; 1.
DR   InterPro; IPR023710; Phosphatase_YcdX_put.
DR   InterPro; IPR004013; PHP_dom.
DR   InterPro; IPR003141; Pol/His_phosphatase_N.
DR   InterPro; IPR016195; Pol/histidinol_Pase-like.
DR   PANTHER; PTHR36928; PHOSPHATASE YCDX-RELATED; 1.
DR   PANTHER; PTHR36928:SF1; PHOSPHATASE YCDX-RELATED; 1.
DR   Pfam; PF02811; PHP; 1.
DR   SMART; SM00481; POLIIIAc; 1.
DR   SUPFAM; SSF89550; PHP domain-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01561};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01561}; Reference proteome {ECO:0000313|Proteomes:UP000027946};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01561}.
FT   DOMAIN          5..79
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
FT   BINDING         8
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01561"
FT   BINDING         10
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01561"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01561"
FT   BINDING         41
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01561"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01561"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01561"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01561"
FT   BINDING         132
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01561"
FT   BINDING         193
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01561"
FT   BINDING         195
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01561"
SQ   SEQUENCE   252 AA;  27773 MW;  6132207CDC71DCAF CRC64;
     MKFVLDVHCH TIASGHSYST VHDIAREAKN NGIDLFALTD HGPEMPGAPH LYHIKNQRVI
     PRVIDGVIVL RGVEVNIMDY EGELDMRDAD LAELDIVIAS LHHVCINPGT MEQNTNALIK
     AMENKHVDIV GHIGNPLFPI DSEKVVKAAK EHNVLIEINN SSFSVSRDGS KENCSHIARL
     AKENGNMVVL GSDCHIAFDV GNFESAGKLL EVVGIPEENI MNTSVQKLID FLESKGKTGL
     EEIREIIKKS FI
//
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