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Database: UniProt
Entry: D0TLZ0_9BACE
LinkDB: D0TLZ0_9BACE
Original site: D0TLZ0_9BACE 
ID   D0TLZ0_9BACE            Unreviewed;       466 AA.
AC   D0TLZ0;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Alkaline phosphatase family protein {ECO:0000313|EMBL:EEZ05134.1};
GN   ORFNames=HMPREF0102_00133 {ECO:0000313|EMBL:EEZ05134.1};
OS   Bacteroides sp. 2_1_22.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=469588 {ECO:0000313|EMBL:EEZ05134.1, ECO:0000313|Proteomes:UP000005775};
RN   [1] {ECO:0000313|EMBL:EEZ05134.1, ECO:0000313|Proteomes:UP000005775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2_1_22 {ECO:0000313|EMBL:EEZ05134.1,
RC   ECO:0000313|Proteomes:UP000005775};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., Chen Z.,
RA   Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA   McDonald J., Allen-Vercoe E., Strauss J., Ambrose C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Bacteroides sp. strain 2_1_22.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601952-2};
CC       Note=Binds 1 Mg(2+) ion. {ECO:0000256|PIRSR:PIRSR601952-2};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601952-2};
CC       Note=Binds 2 Zn(2+) ions. {ECO:0000256|PIRSR:PIRSR601952-2};
CC   -!- SIMILARITY: Belongs to the alkaline phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00005984, ECO:0000256|RuleBase:RU003946}.
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DR   EMBL; GG705173; EEZ05134.1; -; Genomic_DNA.
DR   RefSeq; WP_004312988.1; NZ_GG705173.1.
DR   AlphaFoldDB; D0TLZ0; -.
DR   HOGENOM; CLU_008539_5_0_10; -.
DR   Proteomes; UP000005775; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   CDD; cd16012; ALP; 1.
DR   Gene3D; 1.10.60.40; -; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR001952; Alkaline_phosphatase.
DR   InterPro; IPR018299; Alkaline_phosphatase_AS.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR   PANTHER; PTHR11596:SF5; ALKALINE PHOSPHATASE; 1.
DR   Pfam; PF00245; Alk_phosphatase; 2.
DR   PRINTS; PR00113; ALKPHPHTASE.
DR   SMART; SM00098; alkPPc; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR601952-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}.
FT   ACT_SITE        80
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         30
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         30
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         131
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         133
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         260
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         265
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         269
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         309
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         429
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   466 AA;  51413 MW;  E31362735A1E9497 CRC64;
     MKKLIYTLFF VFISVVANGQ AKYVFYFIGD GMGVNQVNGT EMYQAEIQNG RIGVEPLLFT
     QFPVATMATT FSAKNSVTDS AAAGTALATG KKTYNHAISV GEDKNAIQTV AEKAKKAGKK
     VGVTTSVSVD HATPAAFYAH QPDRNRYYEI ALDLPKANFD FYAGGGFLKP TTSFDKKEAP
     SIFPIFEEAG YTVARGYNDY KAKAAKAEKM ILIQEEGANP SCLPYAIDRK EGDLTLAQIT
     ESAIDFLTKD NKKGFFLMVE GGKIDWACHA NDAATVFNEV KDMDNAIKVA YEFYKKHPKE
     TLIVVTADHE TGGIVLGTGK YELNLKALQH QKHSADGLSQ RISELRKSKG NKVTWEDMKT
     FLGEEMGFWK QFPISWEQEK KLRDEFEKSF VKNKVVFAES MYSKSEPMAA RAKEVMDEIA
     MVGWVSGGHS AGYVPVFAIG AGSQLFGEKI DNTEIPKRIA KAAGYK
//
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