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Database: UniProt/TrEMBL
Entry: A0A1X9ML45_9BACI
LinkDB: A0A1X9ML45_9BACI
Original site: A0A1X9ML45_9BACI 
ID   A0A1X9ML45_9BACI        Unreviewed;       443 AA.
AC   A0A1X9ML45;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Alkaline phosphatase 4 {ECO:0000313|EMBL:ARK32501.1};
DE            EC=3.1.3.1 {ECO:0000313|EMBL:ARK32501.1};
DE   Flags: Precursor;
GN   Name=phoA_2 {ECO:0000313|EMBL:ARK32501.1};
GN   ORFNames=BkAM31D_23000 {ECO:0000313|EMBL:ARK32501.1};
OS   Halalkalibacter krulwichiae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX   NCBI_TaxID=199441 {ECO:0000313|EMBL:ARK32501.1, ECO:0000313|Proteomes:UP000193006};
RN   [1] {ECO:0000313|EMBL:ARK32501.1, ECO:0000313|Proteomes:UP000193006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM31D {ECO:0000313|EMBL:ARK32501.1,
RC   ECO:0000313|Proteomes:UP000193006};
RA   Krulwich T.A., Anastor L., Ehrlich R., Ehrlich G.D., Janto B.;
RT   "Bacillus krulwichiae AM31D Genome sequencing and assembly.";
RL   Submitted (APR-2017) 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; CP020814; ARK32501.1; -; Genomic_DNA.
DR   RefSeq; WP_066160123.1; NZ_CP020814.1.
DR   AlphaFoldDB; A0A1X9ML45; -.
DR   STRING; 199441.BkAM31D_23000; -.
DR   KEGG; bkw:BkAM31D_23000; -.
DR   Proteomes; UP000193006; 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; 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; 1.
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   Hydrolase {ECO:0000313|EMBL:ARK32501.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000193006};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}.
FT   ACT_SITE        88
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         48
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         48
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         139
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         141
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         265
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         270
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         274
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         312
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         313
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         403
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   443 AA;  47355 MW;  985A9F4CDE056FB1 CRC64;
     MKMFKRFLAT ALCSAVVVSG FSHIQKVDAG PPSHSNAKVD NVIYMIPDGY SASYATNYRI
     YKGEDPVLDS MLVGMMKTNS ADNWVTDSAA AGTAMATGVK TNNGMVSVTP DGEPLETILQ
     AAGDAGKSTG LVATSTITHA TPAVFGSHVE SRGSEADIAL QLANEIDVLL GGGKANFLPK
     SEGGNQEERH LIDEAIENGY QFVETREELL ALNGQADKVL GLFATGAMAP ELDRDVTEEP
     SLAEMTKAAI DTLSKEKDGF FLMVEGSQID WAGHAHDAAW AMKDTEAFEE AVKEALEFAK
     NDRKTLVVVA GDHDTGGMSV GGYDEYLAKA DILHDVTATG NYMASELHAD RSNAKDVLST
     YANIELTAEE EERIQTAPAN QVAFVINTII SERAYVGWSS TAHTGVDVPL YAHGPSSDLF
     NGLLDNTDLP QRMAEAMKID FAQ
//
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