ID S4YLQ2_SERPL Unreviewed; 475 AA.
AC S4YLQ2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:AGP43723.1};
GN ORFNames=M621_07800 {ECO:0000313|EMBL:AGP43723.1};
OS Serratia plymuthica S13.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=1348660 {ECO:0000313|EMBL:AGP43723.1, ECO:0000313|Proteomes:UP000014900};
RN [1] {ECO:0000313|EMBL:AGP43723.1, ECO:0000313|Proteomes:UP000014900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S13 {ECO:0000313|EMBL:AGP43723.1};
RX PubMed=23929484;
RA Muller H., Furnkranz M., Grube M., Berg G.;
RT "Genome Sequence of Serratia plymuthica Strain S13, an Endophyte with
RT Germination- and Plant-Growth-Promoting Activity from the Flower of Styrian
RT Oil Pumpkin.";
RL Genome Announc. 1:e00594-13(2013).
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}.
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; CP006566; AGP43723.1; -; Genomic_DNA.
DR RefSeq; WP_004942302.1; NC_021659.1.
DR AlphaFoldDB; S4YLQ2; -.
DR KEGG; sry:M621_07800; -.
DR PATRIC; fig|1348660.3.peg.1503; -.
DR eggNOG; COG1785; Bacteria.
DR HOGENOM; CLU_008539_0_1_6; -.
DR Proteomes; UP000014900; 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; 2.
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 Disulfide bond {ECO:0000256|PIRSR:PIRSR601952-3};
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 Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..475
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004526403"
FT ACT_SITE 128
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 77
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 348
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 395
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 438
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT DISULFID 194..204
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-3"
FT DISULFID 312..362
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-3"
SQ SEQUENCE 475 AA; 49551 MW; 53705CBD5BE730B9 CRC64;
MLQPVSLIAG AVLSALLCST ALADETPANT AGLSERAARG NIVEPGGARR LSGDQTAALK
ASLSDKTVKN VILLIGDGMG DSEITSARNY AEGAGGYFKG IDALPLTGQY THYSLDKKTH
KPDYVTDSAA SATAWSTGVK TYNGALGVDV NGKDQPTLLE IAKAAGKATG NVSTAELQDA
TPAAQVSHVT SRKCYGPEET SEKCATNALE NGGRGSITEQ LLKTRADVSL GGGAKSFNQL
AKSGEWQGKS LKDQATALGY QWVENLDGLN AISVANQQKP LLGLFAAGNM PVRWQGPKAS
HHGNIDQPAV TCENNPARTA DIPTLAAMTE KAIDLLKNQQ NGFFLQVEGA SIDKQDHEAN
PCGQFGETVD LDEAVQKALA FARADGNTLV IVTADHAHSS QIIAVDAKAP GLTQTLTTKD
GAPMTISYGN SEEGSQGHTG TQLRVAAYGP HAANVVGLTD QTDLFYTMRD AMAIK
//
