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Database: UniProt
Entry: A0A142XKS2_9BACT
LinkDB: A0A142XKS2_9BACT
Original site: A0A142XKS2_9BACT 
ID   A0A142XKS2_9BACT        Unreviewed;       567 AA.
AC   A0A142XKS2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Alkaline phosphatase PhoV {ECO:0000313|EMBL:AMV27262.1};
DE            EC=3.1.3.1 {ECO:0000313|EMBL:AMV27262.1};
DE   Flags: Precursor;
GN   Name=phoV_3 {ECO:0000313|EMBL:AMV27262.1};
GN   ORFNames=VT84_22865 {ECO:0000313|EMBL:AMV27262.1};
OS   Gemmata sp. SH-PL17.
OC   Bacteria; Planctomycetota; Planctomycetia; Gemmatales; Gemmataceae;
OC   Gemmata.
OX   NCBI_TaxID=1630693 {ECO:0000313|EMBL:AMV27262.1, ECO:0000313|Proteomes:UP000076098};
RN   [1] {ECO:0000313|EMBL:AMV27262.1, ECO:0000313|Proteomes:UP000076098}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH-PL17 {ECO:0000313|EMBL:AMV27262.1,
RC   ECO:0000313|Proteomes:UP000076098};
RA   van der Voort M., Raaijmakers J.M.;
RT   "Genome minning of novel planctomycete species.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP011271; AMV27262.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A142XKS2; -.
DR   STRING; 1630693.VT84_22865; -.
DR   KEGG; ges:VT84_22865; -.
DR   Proteomes; UP000076098; Chromosome.
DR   GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd16016; AP-SPAP; 1.
DR   Gene3D; 3.30.1360.150; -; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR026263; Alkaline_phosphatase_prok.
DR   InterPro; IPR002591; Phosphodiest/P_Trfase.
DR   PANTHER; PTHR10151:SF120; BIS(5'-ADENOSYL)-TRIPHOSPHATASE; 1.
DR   PANTHER; PTHR10151; ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE; 1.
DR   Pfam; PF01663; Phosphodiest; 1.
DR   PIRSF; PIRSF031924; Pi-irrepressible_AP; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:AMV27262.1};
KW   Phosphoprotein {ECO:0000256|PIRSR:PIRSR031924-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076098};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..567
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007504281"
FT   REGION          114..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        79
FT                   /note="Phosphothreonine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031924-50"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031924-51"
FT   BINDING         172..174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031924-51"
SQ   SEQUENCE   567 AA;  60778 MW;  EAFC1F93189D1AD8 CRC64;
     MRLLCLLAAI LLAALLLAPD TVAEESTHPR LVVLVYFDQF RGDYLARWKD EFGEGGFKRI
     TTDGAWFQNC HYPYAYTVTA AGHSSVATGC VPSVHGVIGN DWYDRGVGKT VNCVGSDRHE
     QVPGRTAEGT DSDEKKGAKG GVSPERLLKP TIADAIKLGT DGKGKVVALS LKNRGAALPG
     GRAPDVCYWM DGGTGQFVTS TYYREAVHPW VAAFNKSKPA ERWRGKTWDR FRTDIDYAKL
     SGPDDIAGES KGASGQGRVF PHPFEPTDPK AKPAYLNAVY TSPFGNDLLL DLAERAISAE
     GLGKDDVPDL LSLSFSSNDA VGHAWGPDSQ EVLDVTLRSD RIMKRLLEVL DAKVGRGKYV
     LAMTADHGIC PLPEVSRKQG KDAARVQPAL SAKVEAFLVE KYGKTAAKWV EASSGPWLYL
     NAKAVTAAGV KQADVEAELA QWLAKRDGVE AVYTRTALTA GIPPTDATGE MVARSFRAER
     CGDVYVLLKP YYLPTAVLDT GTTHGSPWEY DTHVPLVVYG TGVVPGVHTG RVTPLATAAI
     LSTAAGVKAP SGATAPVPTG LFVPHRK
//
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