ID A0A0Q5N3K2_9MICO Unreviewed; 659 AA.
AC A0A0Q5N3K2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Alkaline phosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASF89_12105 {ECO:0000313|EMBL:KQR63843.1};
OS Frigoribacterium sp. Leaf172.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frigoribacterium.
OX NCBI_TaxID=1736285 {ECO:0000313|EMBL:KQR63843.1, ECO:0000313|Proteomes:UP000051720};
RN [1] {ECO:0000313|EMBL:KQR63843.1, ECO:0000313|Proteomes:UP000051720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf172 {ECO:0000313|EMBL:KQR63843.1,
RC ECO:0000313|Proteomes:UP000051720};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR63843.1, ECO:0000313|Proteomes:UP000051720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf172 {ECO:0000313|EMBL:KQR63843.1,
RC ECO:0000313|Proteomes:UP000051720};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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 -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000256|ARBA:ARBA00004191}.
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:KQR63843.1}.
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DR EMBL; LMPB01000003; KQR63843.1; -; Genomic_DNA.
DR RefSeq; WP_055815126.1; NZ_LMPB01000003.1.
DR AlphaFoldDB; A0A0Q5N3K2; -.
DR STRING; 1736285.ASF89_12105; -.
DR Proteomes; UP000051720; 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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601952-3};
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:UP000051720};
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..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..659
FT /note="Alkaline phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006257197"
FT TRANSMEM 621..640
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 576..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 127
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 73
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 345
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT DISULFID 193..202
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-3"
FT DISULFID 309..359
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-3"
SQ SEQUENCE 659 AA; 65655 MW; D4A2198C890A7ECF CRC64;
MTPTTRRRRA ALITGAVAIS ASLALAPAVA SAATPSDVAE NGGAARSIDD STQVLLDSVK
AGPAKNVILL IGDGMGDSEI TSARNYAYGA GGQLPGIDAL PLTGQYTTYS LYRDGANKGE
PDYVPDSAAT GSAWATGTKT YDNAISVDID GVPQDTLLEI AKANGKKTGN VSTAELQDAT
PAVQAAHVAA RSCYGPDSVT QCGADALDQG GLGSISEQII GTRADVTLGG GAASFTQTAR
AGQWQGETLF DQAADRGYQI VRDAAGLDAV AAAGQAAPVL GTFTDGNFPT RFAATTATVG
GADLAPQTCT PNPERLPTDL SLRSLTEKSI DLLDTGDQGF FLQVEGASID KRDHSADACG
QIGEVLDLDE AVRAALDFAI ADGDTMVIVT ADHAHTSQIV DSTPPATLST ALTTVDGTTM
KIAYGTAAAG GSQQHTGSQL RVAGYGPGAG NVVGLIDQTD NFFTISNALE LDRDLDGLSA
AATVSAPSEV APESSFTVSG AGLNGDRQVR AVLDAGDGAD PVDLGLSDVV DGTVTLTATA
PAEAGNATVT LTGVQSGVTA SAVVAVVDGA VAPVPTATPA PGDPSATPTD PAGVVPVGDD
GSAGGAGTAG SGPLAFTGSE ALPALVLALM LVVSGAVLVA RRRRQQQLAS ANGDLGPQL
//