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Database: UniProt
Entry: A0A0M9GS04_9BACI
LinkDB: A0A0M9GS04_9BACI
Original site: A0A0M9GS04_9BACI 
ID   A0A0M9GS04_9BACI        Unreviewed;       469 AA.
AC   A0A0M9GS04;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:KPB04056.1};
GN   ORFNames=AAV98_13565 {ECO:0000313|EMBL:KPB04056.1};
OS   Bacillus sp. CHD6a.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1643452 {ECO:0000313|EMBL:KPB04056.1, ECO:0000313|Proteomes:UP000037908};
RN   [1] {ECO:0000313|EMBL:KPB04056.1, ECO:0000313|Proteomes:UP000037908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHD6a {ECO:0000313|EMBL:KPB04056.1,
RC   ECO:0000313|Proteomes:UP000037908};
RA   Lin W., Liu Y., Zheng Q., Jiao N.;
RT   "Genome sequence of Bacillus sp. CHD6a isolated from the shallow-sea
RT   hydrothermal environment.";
RL   Submitted (APR-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPB04056.1}.
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DR   EMBL; LBMD01000017; KPB04056.1; -; Genomic_DNA.
DR   RefSeq; WP_060666098.1; NZ_LBMD01000017.1.
DR   AlphaFoldDB; A0A0M9GS04; -.
DR   STRING; 1643452.AAV98_13565; -.
DR   PATRIC; fig|1643452.3.peg.1573; -.
DR   OrthoDB; 9794455at2; -.
DR   Proteomes; UP000037908; 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; 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   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..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..469
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005836600"
FT   ACT_SITE        96
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         47
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         47
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         147
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         149
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         270
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         275
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         279
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         317
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         318
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         412
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   469 AA;  51547 MW;  AB2244A24BAE12A2 CRC64;
     MFSKKLLTVT MAASLAVSGF AINQASADKD KGASKDEIRN VIFLIGDGMG NSYTSAHRTL
     NNDPNTPEME ETAYDPYLVG MQSTHSSDEE ESVTDSAAAA TSMSAGIKTY NGAIAVDMEK
     EDVKTVLEQA KENGKSTGLV ATSQINHATP AAFGAHDESR NNYNQIADDY YDDLINGKHK
     VDVLLGGGTN YFVRGDRDLT KEFQKDGYSY VTTRDEMLND DNEQVLGLFA PKGLEKMIDR
     SEEQPSLKEM TNSALDRLDN NKKGFFLMVE GSQIDWAGHD NDIVGAMSDM QDFEQAFQAA
     IDFAKKDKHT LVIATADHST GGMAMGRDGE YKWDPTAIKA AKKTPDFIAK KIVEGAPVEE
     TLKEYIDLEL TPEEIQSVKD AKETSGELTE IDNAIERIFD LRTGTGWTTD GHTGEDVQVY
     AYGPGMNKFT GKIDNTDTAK EIFNILKKTK NGHADTDHRE GEKDEHDND
//
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