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Database: UniProt
Entry: A0A0Q5N3K2_9MICO
LinkDB: A0A0Q5N3K2_9MICO
Original site: A0A0Q5N3K2_9MICO 
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
//
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