ID A0A0Q5LER7_9MICO Unreviewed; 640 AA.
AC A0A0Q5LER7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Alkaline phosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASF82_01100 {ECO:0000313|EMBL:KQR47210.1};
OS Frigoribacterium sp. Leaf164.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frigoribacterium.
OX NCBI_TaxID=1736282 {ECO:0000313|EMBL:KQR47210.1, ECO:0000313|Proteomes:UP000051005};
RN [1] {ECO:0000313|EMBL:KQR47210.1, ECO:0000313|Proteomes:UP000051005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf164 {ECO:0000313|EMBL:KQR47210.1,
RC ECO:0000313|Proteomes:UP000051005};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR47210.1, ECO:0000313|Proteomes:UP000051005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf164 {ECO:0000313|EMBL:KQR47210.1,
RC ECO:0000313|Proteomes:UP000051005};
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 -!- 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:KQR47210.1}.
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; LMOX01000001; KQR47210.1; -; Genomic_DNA.
DR RefSeq; WP_056055525.1; NZ_LMOX01000001.1.
DR AlphaFoldDB; A0A0Q5LER7; -.
DR STRING; 1736282.ASF82_01100; -.
DR OrthoDB; 9794455at2; -.
DR Proteomes; UP000051005; 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 PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 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:UP000051005};
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..640
FT /note="Alkaline phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006255562"
FT TRANSMEM 606..625
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 566..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 123
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 174
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 340
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 388
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT DISULFID 189..198
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-3"
FT DISULFID 305..354
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-3"
SQ SEQUENCE 640 AA; 63638 MW; 72D6EFBFD7E4908E CRC64;
MSSTTRRTRA ALATGAMALA ASVALLPGAA FAATPADVAE NGGAARSSDD STQALLDSVQ
AGPAKNVILL IGDGMGDSEI TSARNYQYGA GGELPGIDAL PLTGQYTTYS LTKAGKPDYV
PDSAATGSAW ATGTKTYDNA VSVDIAGTPQ DTLVEIAKAN GKKTGNVSTA EIQDATPAVQ
AAHVAARSCY GPDSVTQCGA DALDQGGLGS ISEQIIGTRA DLTLGGGSAS FRQSARAGQY
QGESLFDQAA DRGYQVVGDA AGLGALTAAD QASPVLGTFT DGNFPTRFAP STATVGGADL
APQACTPNPA RLSTDLSLRS LTEKSIDLLD GDQGFFLQVE GASIDKRDHS ADACGQIGEV
LDLDEAVQAA LEFAKADGNT MVIVTADHAH TSQIVDSTPP ATLSTALLTT EGSTMKIAYG
TAAAGGSQQH TGTQLRVAGY GPGAANVVGL IDQTDNFFTI VNALELDRDL DGLSADGTVS
APAEVAPGTD FTVTASGVEG DRQVSGVYTP ASGDPVDLGY VDVVDGVATF TVTAPTALGA
GSVTLVGVQS GVELRADVLV AAGAPTPAPT ASPTPAAVPG GSGTGAGGAG TTASGSGPLA
FTGSDMVPAL LLALMLAGTG AVLVARRRRR SVLDHSGAQL
//
