ID A0A180FV10_9BACT Unreviewed; 567 AA.
AC A0A180FV10;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Alkaline phosphatase 4 {ECO:0000313|EMBL:OAV75721.1};
DE EC=3.1.3.1 {ECO:0000313|EMBL:OAV75721.1};
GN Name=phoA {ECO:0000313|EMBL:OAV75721.1};
GN ORFNames=Barb7_00638 {ECO:0000313|EMBL:OAV75721.1};
OS Bacteroidales bacterium Barb7.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1633203 {ECO:0000313|EMBL:OAV75721.1, ECO:0000313|Proteomes:UP000078281};
RN [1] {ECO:0000313|EMBL:OAV75721.1, ECO:0000313|Proteomes:UP000078281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Barb7 {ECO:0000313|EMBL:OAV75721.1,
RC ECO:0000313|Proteomes:UP000078281};
RA Tai V., Carpenter K.J., Weber P.K., Nalepa C.A., Perlman S.J.,
RA Keeling P.J.;
RT "Genomic and NanoSIMS analyses of nitrogen-fixing bacterial ectosymbionts
RT of a protist inhabiting a wood-eating cockroach.";
RL Submitted (DEC-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|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:OAV75721.1}.
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DR EMBL; LBCZ01000047; OAV75721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A180FV10; -.
DR PATRIC; fig|1633203.3.peg.2445; -.
DR Proteomes; UP000078281; 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; 1.10.60.40; -; 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 PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:OAV75721.1};
KW Magnesium {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:UP000078281};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..567
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008109420"
FT ACT_SITE 85
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 39
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 268
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 567 AA; 62644 MW; 06546FD6A746303D CRC64;
MNKKQMYFFL LTAWLVLPAG AVTPEKVRAV KNLIIMIPDG TSLPVVSISR WTQWYANPDK
PDLNIDPYLC GTVSTFSSNA PIGDSAPTTS CYMTGYPSRT GYVSTYPEQD RENDIYPTDP
ARAYQPLTTV LEAAKMTQGK AVGLVFTCEF PHATPADCSA HSYNRSKYEW IAPQMAHNNL
SVVIGGGVSL LSAGDEEYLK ANGYHIYKDD LNGMRTDTGD KMWALYGSKE MDYDLDRNPD
EQPSLEEMTR KAIGKLSNDP DGFVLMVEGS KVDWAAHAND PVGMVGDFLA FDRACGVALE
FARQNGETAV IILPDHGNSG ISLGRSDCKG YDKLTKDQLF HQFSQYKLTA EGFAKKINET
PYAEVQDIFR TYAGFELSPE ELNALNNCKD YTHSPIPADK RSSEGIQASM YSGSLTSFVA
KLLTSKTCFG FTTGGHTGEE VFIAAYHPQG DIPLGRRTNV ELNKYLCDVL GLPSSLDEIT
GRIFAPHTDV FKGYDCEILP ASDTKPFPTL VVRNRKDSRK QLTISPFTDT VKAGRKGGED
IRLSSVVIYV DKNNTFYLPE SLTGYFK
//
