ID B2FP33_STRMK Unreviewed; 568 AA. AC B2FP33; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 27-MAR-2024, entry version 79. DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:CAQ46887.1}; GN OrderedLocusNames=Smlt3463 {ECO:0000313|EMBL:CAQ46887.1}; OS Stenotrophomonas maltophilia (strain K279a). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group. OX NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ46887.1, ECO:0000313|Proteomes:UP000008840}; RN [1] {ECO:0000313|EMBL:CAQ46887.1, ECO:0000313|Proteomes:UP000008840} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K279a {ECO:0000313|EMBL:CAQ46887.1, RC ECO:0000313|Proteomes:UP000008840}; RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74; RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D., RA Parkhill J., Thomson N.R., Avison M.B.; RT "The complete genome, comparative and functional analysis of RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug RT resistance determinants."; RL Genome Biol. 9:R74.1-R74.13(2008). 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}. 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; AM743169; CAQ46887.1; -; Genomic_DNA. DR RefSeq; WP_005410519.1; NC_010943.1. DR AlphaFoldDB; B2FP33; -. DR EnsemblBacteria; CAQ46887; CAQ46887; Smlt3463. DR KEGG; sml:Smlt3463; -. DR eggNOG; COG1785; Bacteria. DR HOGENOM; CLU_008539_4_1_6; -. DR Proteomes; UP000008840; 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. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000008840}; KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 22..568 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002775930" FT REGION 435..476 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 435..459 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 127 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 187 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 189 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 391 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 499 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" SQ SEQUENCE 568 AA; 60056 MW; 507288E153932FC3 CRC64; MRRSVSLLAA CATTLLLGAC ASTTPATAPA SLKVAVDPVA HPAGETPQWW YRSGAAQAAA NGAMSGKAKN VILFLGDGMS LTTVAASRIY EGQQKGGSGE ENLLSWERFP ATAFSKTYNT DSQTPDSAGT MTAITTGVKT HMGAIGVSAG SRTDCADSLS KGLLTWLQLA DSAGLATGVV STARLTHATP AATYAHSPER NWENDTDLTE AAKAAGCKDI AQQLLSTSRY GRGPLVALGG GRGEFTTVEE RDPEYDDKVG QRLDGRSLVQ EWQQAHPQGA YVWNSKQLAA AANAPAILGL FEPDHMRYEY ERPQDPGGEP SLAELTAAAI KNLAKHQEGY VLMIEGARID HANHSGNAYR ALTETVALSD AVRVANELTS ADDTLIIVTA DHSHTLNFVG YPARGNPILG KVKDKGGEDG AGKLDYALDG TGQPYTTLSY ANGPGHTGSS NQQPAGPKRY PHNPSSFEPA NGRPNLREVD TEHPDYMQEA LVPMKSESHG GEDVGIWARG PGSKAIRGTL EQNAIYHMIV QATPALRERL CQAGTCDDKG VPVQLPAPTA FERKAEAK //