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}.
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; 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
//