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Database: UniProt
Entry: A0A261FES9_9BIFI
LinkDB: A0A261FES9_9BIFI
Original site: A0A261FES9_9BIFI 
ID   A0A261FES9_9BIFI        Unreviewed;       711 AA.
AC   A0A261FES9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:OZG57657.1};
GN   ORFNames=BTIS_1310 {ECO:0000313|EMBL:OZG57657.1};
OS   Bifidobacterium tissieri.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1630162 {ECO:0000313|EMBL:OZG57657.1, ECO:0000313|Proteomes:UP000216444};
RN   [1] {ECO:0000313|EMBL:OZG57657.1, ECO:0000313|Proteomes:UP000216444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100201 {ECO:0000313|EMBL:OZG57657.1,
RC   ECO:0000313|Proteomes:UP000216444};
RX   PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA   Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA   Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA   van Sinderen D., Ventura M.;
RT   "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT   family.";
RL   BMC Genomics 18:568-568(2017).
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   -!- 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:OZG57657.1}.
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DR   EMBL; MWWV01000007; OZG57657.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261FES9; -.
DR   Proteomes; UP000216444; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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   SMART; SM00098; alkPPc; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|PIRSR:PIRSR601952-2};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216444};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..711
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012514785"
FT   TRANSMEM        683..703
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          470..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          644..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..665
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        147
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         67
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         198
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         200
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         393
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         398
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         402
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         439
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         440
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         504
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   711 AA;  73202 MW;  A83A9B5E5A8A9721 CRC64;
     MEVNTRKALK GTVAAILASA TLFGFAGLAN AADGQGVEQL KEHGAAQRIA GVYGNAKAKN
     VILFIGDGMG DSEITVARNY LHGVNGSFDG LDKIGQPNLN KGVETGTGQY TTFSLGNSSN
     DSLMAKDKNG QLTGSKTAGV ITPVTDSSAS GSSWATGTKT YNNAVDVDVE GNPQLNLIEL
     AKAAGKATGN VTTAEIQDAT PAVLESHSSE RACYGPQGKW DGTDKNGDGV VDLKDAEAAG
     IGSCLAPQLK ANGGIGSISE QLIDTRADVT IGGGAKYFNQ LDQSGKTLWQ AAADQGFQTV
     KSGEVDGFKA LSEANQDKPV LALLGDGNLP TEFNPSVATK QDPAKDANPT ECTVNEKWLG
     NKGASLADFT DKAIDLLQNN KNGKDNGFFL QVEGASIDKQ DHNANACGQI GETDDLDKAI
     SAALNKVDLS DTLIIVTADH AHTSQIVESQ PIYALSTVLK NRDGSKTTIS YGTSEEDLYG
     NGQDTSGDVE GKADPSKAQG NMSHTGTQLR IAASGPGASR VDGLTDQTDN FYTIAHALGL
     ATEKADQDKL SDGASVTAKD NKNQVFDIAG FNGDAVLRYE LKDKDGKVVS ASDATTPLSG
     LRVKTAGVTT IDLSKFITSD AKYSLTVTGQ QSGKTVEIKD FAGPNGTEGN GAAQVGPNAS
     SDKPVASGKV NAPKQNGVLG KTGATVLGVA LLAMALVAGG LAIKFAKSRN A
//
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