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Database: UniProt
Entry: S4YXS9_SERPL
LinkDB: S4YXS9_SERPL
Original site: S4YXS9_SERPL 
ID   S4YXS9_SERPL            Unreviewed;       510 AA.
AC   S4YXS9;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:AGP47373.1};
GN   ORFNames=M621_22315 {ECO:0000313|EMBL:AGP47373.1};
OS   Serratia plymuthica S13.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=1348660 {ECO:0000313|EMBL:AGP47373.1, ECO:0000313|Proteomes:UP000014900};
RN   [1] {ECO:0000313|EMBL:AGP47373.1, ECO:0000313|Proteomes:UP000014900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S13 {ECO:0000313|EMBL:AGP47373.1};
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|RuleBase:RU003946}.
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DR   EMBL; CP006566; AGP47373.1; -; Genomic_DNA.
DR   RefSeq; WP_006328183.1; NC_021659.1.
DR   AlphaFoldDB; S4YXS9; -.
DR   KEGG; sry:M621_22315; -.
DR   PATRIC; fig|1348660.3.peg.4369; -.
DR   eggNOG; COG1785; Bacteria.
DR   HOGENOM; CLU_008539_4_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; 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   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..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..510
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004526583"
FT   ACT_SITE        119
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         69
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
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         182
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         386
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         467
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   510 AA;  54988 MW;  68EFF448BE48F612 CRC64;
     MFRSTLATHL ALSVTLCTGW VATVCAEEKA QLVQREDPYF KQAQEQLQQR LAQPKNTHRA
     KNVILVVGDG MGFSTVTAAR IFEGQQRGVD GESNVLAWEA FPYLAAAKTY SANAQITDSA
     PSAVAMTTGV KTLNDLMGLD HTASLNNCED QKTKTVTTLW EMAASLGMST GAVTTATITH
     ATPGATYAHI ANRDWESDAK MPAEALAAGC SDIARQLVEM KYGNGLNVAM GGGRANFLPE
     SATDPEYAAK KGNRKDGRDL TQAWLKRYGE RGSYVWNQSQ FDRIDPAKVD HLLALFEPSH
     MNFDHDRRED AAGEPSLAEM TGKAIDILAR NPEGYLLLVE GGRIDHGSHN GNAYRTLTDT
     VALNEAVKTI IGKVDLNETL VVVTGDHSHT LTLAGYAKRG NPILGISIGV NGKPLLGSDG
     KPYTTVSFAN GPGGVIPLPE RPALTMEQAS APDFIQPALV PMKSETHGGE DLGIYAIGPW
     SHLFQGTVEE NYTFHVMNYA SRIGERLSNL
//
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