ID   B2I7B3_XYLF2            Unreviewed;       565 AA.
AC   B2I7B3;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:ACB93010.1};
DE            EC=3.1.3.1 {ECO:0000313|EMBL:ACB93010.1};
GN   OrderedLocusNames=XfasM23_1602 {ECO:0000313|EMBL:ACB93010.1};
OS   Xylella fastidiosa (strain M23).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=405441 {ECO:0000313|EMBL:ACB93010.1, ECO:0000313|Proteomes:UP000001698};
RN   [1] {ECO:0000313|EMBL:ACB93010.1, ECO:0000313|Proteomes:UP000001698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M23 {ECO:0000313|EMBL:ACB93010.1,
RC   ECO:0000313|Proteomes:UP000001698};
RX   PubMed=20601474; DOI=10.1128/JB.00651-10;
RA   Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT   "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT   causing almond leaf scorch disease in California.";
RL   J. Bacteriol. 192:4534-4534(2010).
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; CP001011; ACB93010.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2I7B3; -.
DR   KEGG; xfn:XfasM23_1602; -.
DR   HOGENOM; CLU_008539_4_1_6; -.
DR   Proteomes; UP000001698; Chromosome.
DR   GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF5; 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   Hydrolase {ECO:0000313|EMBL:ACB93010.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR601952-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..565
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002778541"
FT   ACT_SITE        125
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         75
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         185
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         187
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         343
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         348
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         352
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         388
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         389
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         495
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   565 AA;  60738 MW;  5124852217147629 CRC64;
     MFRRFSTFLI LPVVSFAIAV SFPSAATSTT QLSVPKVTPP AAETPQWWYQ SGATRAAANG
     AMAGKAKNVI LFLGDGMSFT TVAAARILEG QRNAATGEEN VLSWEHFPAT AFSKTYNTDA
     QTADSAGSMT AITSGVKTHR GAIGVSAGQR NDCVDSLGKS LLTWLTLADS AGMATGIITT
     TRITHATPAA LYAHTPERHW ESDANLPEAA KAGGCRDIAQ QLLTSTRYGR GPLVVLGGGR
     AQFMPAHQHD PEYAERTGLR LDGRDLIEEW KRAHPNGAYV WNTHQFNADA GAPALLGLFE
     PSHMQFEHDR DRHPNGEPSL AEMTRTAIQS LSRDPHGFVL MVEGGRIDHA HHAGNAYRAL
     DETIALSDAV RAAVQTAPKD TLIIVTADHA HTLNFVGYPV RGNPILGKVR SSSRDAGDRT
     QYAHDLNALP YTTLTYANGP GHTAASNTQS AGTKHFNHQP STYELVRGRP DLTTIDTQAP
     DYLQEALVPL KKESHSGEDV GIWATGPGSA AFRGVLEQHV IYHVIVQATP ALRQRLCAAG
     TCNAAGVPIK LPQLADFERK DQSRE
//