ID A0A077KPD4_9FLAO Unreviewed; 608 AA.
AC A0A077KPD4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:BAP33641.1};
GN ORFNames=CHSO_4604 {ECO:0000313|EMBL:BAP33641.1};
OS Chryseobacterium sp. StRB126.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=878220 {ECO:0000313|EMBL:BAP33641.1, ECO:0000313|Proteomes:UP000031650};
RN [1] {ECO:0000313|EMBL:BAP33641.1, ECO:0000313|Proteomes:UP000031650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StRB126 {ECO:0000313|EMBL:BAP33641.1,
RC ECO:0000313|Proteomes:UP000031650};
RX PubMed=25291777; DOI=10.1128/genomeA.00952-14;
RA Morohoshi T., Wang W.Z., Someya N., Ikeda T.;
RT "Complete Genome Sequence of Chryseobacterium sp. Strain StRB126, an N-
RT Acylhomoserine Lactone-Degrading Bacterium Isolated from Potato Root.";
RL Genome Announc. 2:e00952-14(2014).
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}.
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DR EMBL; AP014624; BAP33641.1; -; Genomic_DNA.
DR RefSeq; WP_045501248.1; NZ_AP014624.1.
DR AlphaFoldDB; A0A077KPD4; -.
DR KEGG; chz:CHSO_4604; -.
DR HOGENOM; CLU_445393_0_0_10; -.
DR OrthoDB; 9794455at2; -.
DR Proteomes; UP000031650; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd16012; ALP; 1.
DR CDD; cd08577; PI-PLCc_GDPD_SF_unchar3; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR InterPro; IPR039559; AIM6_PI-PLC-like_dom.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR PANTHER; PTHR11596:SF5; ALKALINE PHOSPHATASE; 1.
DR Pfam; PF00245; Alk_phosphatase; 2.
DR PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|PIRSR:PIRSR601952-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..608
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001719714"
FT ACT_SITE 335
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 386
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 388
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 496
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 501
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 505
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 543
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 544
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 608 AA; 67312 MW; F06C828E71556EEE CRC64;
MKLSKILGLL ALAVFSENQA QNYLNYNVEN AHSHNDYMQE IPFWQAYYAN FGSIEADVFL
VKGKLWVAHT EKELSADRTL ENLYLDNISK QIKQNKGNIY KDTNKKLQLL IDIKQDYKTT
LTALVNTLKK YPEITGNSGV KIVITGGRPQ PGDFKNYPNY LYFDGDLSKD YSADQLKRIG
MFSADLPELV KWNGKGIPRD EETEKIKKAV DKAHAQQKPM RFYGAPDFPN AWVNLMDMGV
DYINTDHIPD LKKFMNTIPK NFYKNTKEYA TYTPTYKTDG ISKKVKNVIL LIPDGTSLPQ
YYAAFTANKG KLNVFNMKST GLSKTNSSNA YVTDSAPGST AFATGVKTKN TFVGVDGAGK
SIAQIPDIIA AKGLVSGLIS TGDVTDATPA DFYAHSDNRN SSEPILKDFA ASKAKILIGG
PTSGLTQDTE QKLKEAKVDI YHSLKSTEKS NNRTLIIDPL ASQRITNGRG NWLADAFDLT
LNDLKNNKKG FFMMVEASQT DGGGHSNNIE QLVTELLDFD HVVGKAMKFA DENKETLVVV
VGDHETGGLT LLDGSLKDGW VFGNFSTNDH TSIPSSVFAY GPNSKEFTGL FENTEIFNKI
MAAYGIEK
//
