ID E0RT33_SPITD Unreviewed; 486 AA.
AC E0RT33;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:ADN02170.1};
DE EC=3.1.3.1 {ECO:0000313|EMBL:ADN02170.1};
GN OrderedLocusNames=STHERM_c12290 {ECO:0000313|EMBL:ADN02170.1};
OS Spirochaeta thermophila (strain ATCC 49972 / DSM 6192 / RI 19.B1).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Spirochaeta.
OX NCBI_TaxID=665571 {ECO:0000313|EMBL:ADN02170.1, ECO:0000313|Proteomes:UP000001296};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 6192;
RA Angelov A., Mientus M., Wittenberg S., Lehmann R., Liesegang H., Daniel R.,
RA Liebl W.;
RT "The genome sequence of Spirochaeta thermophila DSM6192.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADN02170.1, ECO:0000313|Proteomes:UP000001296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49972 / DSM 6192 / RI 19.B1
RC {ECO:0000313|Proteomes:UP000001296};
RX PubMed=20935097; DOI=10.1128/JB.01023-10;
RA Angelov A., Liebl S., Ballschmiter M., Bomeke M., Lehmann R., Liesegang H.,
RA Daniel R., Liebl W.;
RT "Genome sequence of the polysaccharide-degrading, thermophilic anaerobe
RT Spirochaeta thermophila DSM 6192.";
RL J. Bacteriol. 192:6492-6493(2010).
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; CP001698; ADN02170.1; -; Genomic_DNA.
DR RefSeq; WP_013314011.1; NC_014484.1.
DR AlphaFoldDB; E0RT33; -.
DR PaxDb; 665571-STHERM_c12290; -.
DR KEGG; sta:STHERM_c12290; -.
DR eggNOG; COG1785; Bacteria.
DR HOGENOM; CLU_008539_5_0_12; -.
DR Proteomes; UP000001296; Chromosome.
DR GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16012; ALP; 1.
DR Gene3D; 1.10.60.40; -; 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 Hydrolase {ECO:0000313|EMBL:ADN02170.1};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..486
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003139773"
FT ACT_SITE 98
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 49
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 448
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 486 AA; 52625 MW; 53D6820D9D813F93 CRC64;
MKKLIVSLLL LVSLLPMGAG GTRETGSAPE VSPEPSQPKV KYIFFFIGDG MGLPQINAAE
AYLMAREQKD APVRLSFTAF PATGMATTYS SDSYITDSAA AGTALAAGRK TANGVINMDP
GKTRTFTTIA ERLHERGLKV GIISTVSIDH ATPASFYAHQ PSRSNYYEIG LELVKSGFEF
FGGGGFRDPE GKRSKREGGK SNVLEEARKA GYTILTTEEE ILGLSPGSAQ KVIAINPVLP
SSAAMPYKID RDEESLDLAD FTRKAVEFLD NPEGFFIMVE GGKIDWACHA NDAVAAIQDV
LDFDEAVQVA VEFARRHPDE TLIVVTGDHE TGGLTIGFAG TRYENAFPVL LNQKVSFEGF
NAVFESYKGK KALTLDEVMP LVREYFGIES LTPYEEEVLS SALRASLEGV PEDDPQSYLL
YGGYEPFTVT LTHVVNNRAG LGWTTWSHTG VPVPVYATGP GAHLFTGYYD NTDIPKQIAR
LAGVDL
//
