ID A0A0P0GNF2_9BACE Unreviewed; 466 AA.
AC A0A0P0GNF2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:ALJ59434.1, ECO:0000313|EMBL:KAA5413360.1};
DE EC=3.1.3.1 {ECO:0000313|EMBL:ALJ59434.1};
GN Name=phoB_2 {ECO:0000313|EMBL:ALJ59434.1};
GN ORFNames=BcellWH2_02193 {ECO:0000313|EMBL:ALJ59434.1}, DWW88_07275
GN {ECO:0000313|EMBL:RGU28865.1}, DWX97_06570
GN {ECO:0000313|EMBL:RGS38630.1}, F2Y81_23155
GN {ECO:0000313|EMBL:KAA5413360.1}, F2Y87_09445
GN {ECO:0000313|EMBL:KAA5419760.1};
OS Bacteroides cellulosilyticus.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=246787 {ECO:0000313|EMBL:ALJ59434.1, ECO:0000313|Proteomes:UP000061809};
RN [1] {ECO:0000313|EMBL:ALJ59434.1, ECO:0000313|Proteomes:UP000061809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH2 {ECO:0000313|EMBL:ALJ59434.1,
RC ECO:0000313|Proteomes:UP000061809};
RX PubMed=26430127;
RA Wu M., McNulty N.P., Rodionov D.A., Khoroshkin M.S., Griffin N.W.,
RA Cheng J., Latreille P., Kerstetter R.A., Terrapon N., Henrissat B.,
RA Osterman A.L., Gordon J.I.;
RT "Genetic determinants of in vivo fitness and diet responsiveness in
RT multiple human gut Bacteroides.";
RL Science 350:AAC5992-AAC5992(2015).
RN [2] {ECO:0000313|Proteomes:UP000283341, ECO:0000313|Proteomes:UP000285677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF17-25 {ECO:0000313|EMBL:RGU28865.1,
RC ECO:0000313|Proteomes:UP000285677}, and AF22-3AC
RC {ECO:0000313|EMBL:RGS38630.1, ECO:0000313|Proteomes:UP000283341};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000448877, ECO:0000313|Proteomes:UP000482653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIOML-A6 {ECO:0000313|EMBL:KAA5413360.1,
RC ECO:0000313|Proteomes:UP000448877}, and BIOML-A8
RC {ECO:0000313|EMBL:KAA5419760.1, ECO:0000313|Proteomes:UP000482653};
RX PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA Xavier R.J., Alm E.J.;
RT "A library of human gut bacterial isolates paired with longitudinal
RT multiomics data enables mechanistic microbiome research.";
RL Nat. Med. 25:1442-1452(2019).
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}.
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DR EMBL; CP012801; ALJ59434.1; -; Genomic_DNA.
DR EMBL; VVYV01000053; KAA5413360.1; -; Genomic_DNA.
DR EMBL; VVYX01000010; KAA5419760.1; -; Genomic_DNA.
DR EMBL; QRVJ01000003; RGS38630.1; -; Genomic_DNA.
DR EMBL; QRXS01000003; RGU28865.1; -; Genomic_DNA.
DR RefSeq; WP_007217044.1; NZ_VVYX01000010.1.
DR AlphaFoldDB; A0A0P0GNF2; -.
DR STRING; 246787.BcellWH2_02193; -.
DR GeneID; 66306445; -.
DR KEGG; bcel:BcellWH2_02193; -.
DR PATRIC; fig|246787.4.peg.2253; -.
DR eggNOG; COG1785; Bacteria.
DR Proteomes; UP000061809; Chromosome.
DR Proteomes; UP000283341; Unassembled WGS sequence.
DR Proteomes; UP000285677; Unassembled WGS sequence.
DR Proteomes; UP000448877; Unassembled WGS sequence.
DR Proteomes; UP000482653; Unassembled WGS sequence.
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; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
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; 2.
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:ALJ59434.1};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..466
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013461319"
FT ACT_SITE 80
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 31
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 269
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 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 466 AA; 51110 MW; B33D30CC4886FE77 CRC64;
MKRFMYVLLF VLLTGATYAQ QAKYVFYFIG DGMGVNQVNG TEMYLAEQEG RIGVTPLLFT
QFPAVGVATT FSATNSVTDS SAAGTALATG VKTYNGAIGM DDQKNVIQSV AEKAKKAGKK
VGVTTSVSVD HATPAAFYAH QPNRSMYYEI ALDLPKANFD FYAGGGFLKP TTTADKKEAP
SIFPIIEEAG YTIAKGIDDF KVKSTQADKM ILIQKDGANP SCLPYSIDRK DGDMTLAEIT
ESAVSFLTKG KNKGFFLMVE GGKIDWACHS NDPATVFEEV IDMDNAIKVA YEFYKKHPKE
TLIVVTADHE TGGLGLGTGK YELHLKALKN QKQSQDLLST AITDLRKAKG HNVTWEDAKA
LLVEKMGFWK ELPLTWEQEK MLRDEFEQSF VKNKVVFEET LYSKTEPLAA TARKVMSQIA
MIGWTSGSHT AEYVPVYAVG AGSKEFAGKY DNTEIPKRIA KVAGYK
//
