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Database: UniProt
Entry: A0A1E8GPF9_9LACT
LinkDB: A0A1E8GPF9_9LACT
Original site: A0A1E8GPF9_9LACT 
ID   A0A1E8GPF9_9LACT        Unreviewed;       461 AA.
AC   A0A1E8GPF9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:OFI50097.1};
GN   ORFNames=BG261_10340 {ECO:0000313|EMBL:OFI50097.1};
OS   Floricoccus tropicus.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Floricoccus.
OX   NCBI_TaxID=1859473 {ECO:0000313|EMBL:OFI50097.1, ECO:0000313|Proteomes:UP000178622};
RN   [1] {ECO:0000313|Proteomes:UP000178622}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DF1 {ECO:0000313|Proteomes:UP000178622};
RA   Chuah L.-O., Yap K.-P., Thong K.L., Liong M.T., Ahmad R., Rusul G.;
RT   "Draft genome sequence of a novel species of the family Streptococcaceae
RT   isolated from flowers.";
RL   Submitted (SEP-2016) 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:OFI50097.1}.
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DR   EMBL; MKIR01000004; OFI50097.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E8GPF9; -.
DR   STRING; 1859473.BG261_10340; -.
DR   OrthoDB; 9794455at2; -.
DR   Proteomes; UP000178622; 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   Reference proteome {ECO:0000313|Proteomes:UP000178622};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}.
FT   ACT_SITE        87
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         38
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         138
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         140
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         261
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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         270
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         309
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   461 AA;  50311 MW;  3D8C6B07788909DA CRC64;
     MVLAMGTLLT GCASGTGASK SASNSKGKVK NVIFMIGDGM GNSYTSGYRY YKANGGERFV
     SQTEFDKYLI GQQATYPEDP KQNVTDSASA ATAMAAGVKT YNNAIGLDND LSDTESVLER
     AKKKGKSTGL VATSEITHAT PAGYGAHEAT RKSMDRIADD YFDEKIDGKH KIDVLLGGGS
     KLFERDERNL VKEFEKDGYS HVTDKKTLEA DNSDQILGLF ATGGLPKMID RTDETPSLAD
     MTDAAIKRLD KNKDGFFLMV EGSQIDWAGH SNDIVGAMSE MEDFEAAFKK AIEFAEKDGE
     TIVIATADHS TGGLSIAADD VYNWDTKPIH QAKRTPDFMA EEILEKGDVK KTLKDYIEFD
     LTDEEIASVE KTVKDAQELN KTNNEKAVDA VAIPIRKIFD VHSNTGWTTK GHTGEDVNVY
     AFGPQSDLFK GQIENTDQAK LIFGLIEGTN KKEDVKDVEK K
//
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