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Database: UniProt
Entry: W0J4B8_9BACT
LinkDB: W0J4B8_9BACT
Original site: W0J4B8_9BACT 
ID   W0J4B8_9BACT            Unreviewed;       664 AA.
AC   W0J4B8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:AHF91858.1};
GN   ORFNames=OPIT5_18175 {ECO:0000313|EMBL:AHF91858.1};
OS   Opitutaceae bacterium TAV5.
OC   Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX   NCBI_TaxID=794903 {ECO:0000313|EMBL:AHF91858.1, ECO:0000313|Proteomes:UP000003813};
RN   [1] {ECO:0000313|EMBL:AHF91858.1, ECO:0000313|Proteomes:UP000003813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAV5 {ECO:0000313|EMBL:AHF91858.1};
RX   PubMed=25744998;
RA   Kotak M., Isanapong J., Goodwin L., Bruce D., Chen A., Han C.S.,
RA   Huntemann M., Ivanova N., Land M.L., Nolan M., Pati A., Woyke T.,
RA   Rodrigues J.L.;
RT   "Complete Genome Sequence of the Opitutaceae Bacterium Strain TAV5, a
RT   Potential Facultative Methylotroph of the Wood-Feeding Termite
RT   Reticulitermes flavipes.";
RL   Genome Announc. 3:0-0(2015).
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|RuleBase:RU003946}.
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DR   EMBL; CP007053; AHF91858.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0J4B8; -.
DR   STRING; 794903.OPIT5_18175; -.
DR   KEGG; obt:OPIT5_18175; -.
DR   eggNOG; COG1785; Bacteria.
DR   HOGENOM; CLU_008539_3_0_0; -.
DR   Proteomes; UP000003813; Chromosome.
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; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR001952; Alkaline_phosphatase.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR   PANTHER; PTHR11596:SF72; ALKALINE PHOSPHATASE; 1.
DR   Pfam; PF00245; Alk_phosphatase; 1.
DR   PRINTS; PR00113; ALKPHPHTASE.
DR   SMART; SM00098; alkPPc; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|PIRSR:PIRSR601952-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003813};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..664
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004791789"
FT   REGION          578..601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        213
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         164
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         272
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         274
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         449
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         454
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         458
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         496
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         497
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         624
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   664 AA;  69790 MW;  7A724FCF880E22D1 CRC64;
     MNTVTKAFLI RGLAGAALAG AALAPAAALA APVVSRLTPP SLKFSYGDDG APYISRFFID
     QRFDLQATVS PDAGRTITGA KFLVDDVEVP GTVTFIPCNA PGLPADTVAP TLRAYSNTTP
     GVHTLKVVAT QDDDTTVEAE GNFEVVGFTV NGRQAKNVIF MIGDGMGIAH RSAARIMYRG
     IVSGKSLAPL EMDDMPATAL VKTASLNSII TDSAPGAACY SSGNKGNNNQ QGVFPDDTTD
     AFDNPRIELI GEYLARTQQK SLGIVTTADV FDATPGAFGS HTQDRGAGTG ICDGYLDEQA
     VNANLKVLLG GGRKWFLPAG ETGSARSGPT GSTISAELAA AWNLTPGTSD PARDLLSDFE
     DAGFVYTPDR TTLAAIPADT TKLLGLFAFS NMNVAKDKLD GRRGITPAGA TQSVVADYGF
     TDQPLLEEMT DAALRVLNKN RKGFVLMVEG ASIDKQAHNM DTERWITDTI EFDKAIGVAK
     QFAAANPDTL IIVTADHECA GVNIIGASRV TDANLKALAS AGGGAATLRD QVVGTYEVAG
     FPIYTLADDG YPQTTDIDYR MLVGYAANCD RYEDWLTNPR PLRDSQQPLN GEPPLNTYPG
     APVNRDQAGD FFVTGQVPGS QAVHTGSDIP LTATGRASSL FRGVVDNTDV FFLAMQAIHG
     GASY
//
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