ID B4SKN0_STRM5 Unreviewed; 515 AA.
AC B4SKN0;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:ACF53337.1};
DE Flags: Precursor;
GN OrderedLocusNames=Smal_3638 {ECO:0000313|EMBL:ACF53337.1};
OS Stenotrophomonas maltophilia (strain R551-3).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF53337.1, ECO:0000313|Proteomes:UP000001867};
RN [1] {ECO:0000313|EMBL:ACF53337.1, ECO:0000313|Proteomes:UP000001867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R551-3 {ECO:0000313|EMBL:ACF53337.1,
RC ECO:0000313|Proteomes:UP000001867};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; CP001111; ACF53337.1; -; Genomic_DNA.
DR RefSeq; WP_012512260.1; NC_011071.1.
DR AlphaFoldDB; B4SKN0; -.
DR STRING; 391008.Smal_3638; -.
DR KEGG; smt:Smal_3638; -.
DR eggNOG; COG1785; Bacteria.
DR HOGENOM; CLU_008539_7_0_6; -.
DR OrthoDB; 9794455at2; -.
DR Proteomes; UP000001867; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
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; 2.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..515
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002826095"
FT ACT_SITE 133
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 357
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 422
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 515 AA; 55202 MW; 71EB4A7E49AE4417 CRC64;
MTRPVARRWL CPSILAVLAT LSGCQPNLRA DAVPPAEARP HNVIVMINDG AGWGTWDAAA
YWQYGSREGA PYADFPQRLA VATFPLNASS QPTRDNAQTL GYDAAKAWDD SPVPAQDLPF
AGYQYLAAVA TDSAAAGTAL SSGIKTYNNA INYNNDGNAV EFNTLRAKRL GMATGVVTSV
PFAHATPAAF AAQNESRNNY HAIAHQMLAQ GHMDLVMGTG GPGYSVDGRA CGGDAGAAKA
EGCANPWEWV SQQDWQQLQA GTSIGGNPAG PWRLIRSKEE FAALAQGRLP ADRPLIGVPR
VANTLQQARQ LQVVGKDATT PSGVRKIDSV PDLASMTRGA LRFLQQRSSK GLFLMVEGGA
TDWAAHTSAC GTEWHYGQCS DQPQYGRLIE ETVEFNDAVT AVIEWIERNG GWEHTLLIVT
TDHDNSMPMG PDAQSVAFEP VRNNGRGHMP GMSFRPTGNH SNALVPLWAK GAGAELLGKR
VRGVDAGYRQ HVRWNDGSYI DNTDVAAAVQ EALQR
//
