ID   G0AY13_9GAMM            Unreviewed;       439 AA.
AC   G0AY13;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:AEG10121.1};
DE            EC=3.1.3.1 {ECO:0000313|EMBL:AEG10121.1};
DE   Flags: Precursor;
GN   ORFNames=Sbal175_0841 {ECO:0000313|EMBL:AEG10121.1};
OS   Shewanella baltica BA175.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=693974 {ECO:0000313|EMBL:AEG10121.1, ECO:0000313|Proteomes:UP000002249};
RN   [1] {ECO:0000313|EMBL:AEG10121.1, ECO:0000313|Proteomes:UP000002249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BA175 {ECO:0000313|EMBL:AEG10121.1,
RC   ECO:0000313|Proteomes:UP000002249};
RX   PubMed=22328742; DOI=10.1128/JB.06468-11;
RA   Caro-Quintero A., Auchtung J., Deng J., Brettar I., Hofle M., Tiedje J.M.,
RA   Konstantinidis K.T.;
RT   "Genome sequencing of five Shewanella baltica strains recovered from the
RT   oxic-anoxic interface of the Baltic Sea.";
RL   J. Bacteriol. 194:1236-1236(2012).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002767; AEG10121.1; -; Genomic_DNA.
DR   RefSeq; WP_006083001.1; NC_017571.1.
DR   AlphaFoldDB; G0AY13; -.
DR   KEGG; sbb:Sbal175_0841; -.
DR   HOGENOM; CLU_008539_6_2_6; -.
DR   Proteomes; UP000002249; 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:AEG10121.1};
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   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..439
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003397403"
FT   ACT_SITE        93
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         44
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         44
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         144
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         146
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         257
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         262
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         304
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         305
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         397
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   439 AA;  47378 MW;  6DD5F4C27642F8CA CRC64;
     MSFTKAPLLL LGISLLLSTP VWADETGPTK APSRPKNIVI MIGDGMGPSY TSAYRYYKDN
     PDTEEVEQTV FDRLLVGMAS TYPASVSGYV TDSAAAATAL ATGVKSYNGA ISVDTQKQPL
     PTILEKAKSL GLSTGVAVTS QINHATPAAF LAHNESRKNY DALALSYLET NADVFLGGGQ
     KYFPPALLEQ FKAKGYQHIS RFEDLASITQ PKVLGLFAEV QLPWAIDEKD ARKLSTLTQK
     ALSLLSQNDQ GFVLLVEGSL IDWAGHNNDI ATAMGEMDEF SNAIEVVEQF VREHPDTLMV
     ITADHNTGGL SIGVDGNYSW NPEILRNISA STDTLALAAI TGEQWQADLA RGLGFELSEE
     EVAKLNVARM QGLETMAVAI RHVIDKRTDT GWTTDGHTGT DVQVFAAGPA SELFNGHQDN
     TDIANKIFSL LPKPKKPKS
//