ID E3EED6_PAEPS Unreviewed; 436 AA.
AC E3EED6;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:ADO55387.1};
GN Name=phoB1 {ECO:0000313|EMBL:ADO55387.1};
GN ORFNames=PPSC2_06770 {ECO:0000313|EMBL:ADO55387.1};
OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO55387.1, ECO:0000313|Proteomes:UP000006868};
RN [1] {ECO:0000313|EMBL:ADO55387.1, ECO:0000313|Proteomes:UP000006868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:ADO55387.1,
RC ECO:0000313|Proteomes:UP000006868};
RX PubMed=21037012; DOI=10.1128/JB.01234-10;
RA Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT activity.";
RL J. Bacteriol. 193:311-312(2011).
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|ARBA:ARBA00005984, ECO:0000256|RuleBase:RU003946}.
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DR EMBL; CP002213; ADO55387.1; -; Genomic_DNA.
DR RefSeq; WP_013370018.1; NC_014622.2.
DR AlphaFoldDB; E3EED6; -.
DR STRING; 1406.LK13_19735; -.
DR KEGG; ppm:PPSC2_06770; -.
DR PATRIC; fig|886882.15.peg.1394; -.
DR eggNOG; COG1785; Bacteria.
DR HOGENOM; CLU_008539_6_2_9; -.
DR OrthoDB; 9794455at2; -.
DR Proteomes; UP000006868; Chromosome.
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; IPR018299; Alkaline_phosphatase_AS.
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.
DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR601952-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006868};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..436
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003169144"
FT REGION 204..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 111
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 164
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 398
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 436 AA; 45723 MW; 4B8718CAC129EF65 CRC64;
MKKPSMKKSI LALSAVTVLT VPLLSADIPT AFAAATSTKS TVAESKAQKA VSAKADTPKN
VILFIGDGMG EASRNAIRLA TVGKSGLLEM DKMPITGLVS TSSGDNLVTD SAAAATAIAT
GVKTYNGAIG MDLNKKPVTT IMELAKKAGM STGVVTTSQV TDATGAAFGA HVEKRSAQSE
IAKQYLEKSK LDVILGGGED FWYPAGTPGK HPDAPAEDPE EASKGTQGNL VEQAKKLGYS
YVTDQAEMKA AKGSKLLGLF ANEEMFQAHN KLGNSYNPTV SLPDMTAKAI DVLSKNKKGF
FLMVEEEGTD EMAHDNEGEL TIKAGQQLDK AVKVAKDYAK AHPDTLVLVT ADHETGGLAI
EGEDAEDESG EGVSKEDGPF TVKGSDEKFY IDWTTGGHTS VDVALTAMGP GSSQFSGNYP
NTAIHDKLVK LLQLKK
//
