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Database: UniProt
Entry: A5ILE4_THEP1
LinkDB: A5ILE4_THEP1
Original site: A5ILE4_THEP1 
ID   A5ILE4_THEP1            Unreviewed;       593 AA.
AC   A5ILE4;
DT   26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Sulfatase {ECO:0000313|EMBL:ABQ47017.1};
GN   OrderedLocusNames=Tpet_0999 {ECO:0000313|EMBL:ABQ47017.1};
OS   Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 /
OS   RKU-1).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC   Thermotoga.
OX   NCBI_TaxID=390874 {ECO:0000313|EMBL:ABQ47017.1, ECO:0000313|Proteomes:UP000006558};
RN   [1] {ECO:0000313|Proteomes:UP000006558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1
RC   {ECO:0000313|Proteomes:UP000006558};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Thermotoga petrophila RKU-1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABQ47017.1, ECO:0000313|Proteomes:UP000006558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1
RC   {ECO:0000313|Proteomes:UP000006558};
RX   PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA   Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA   DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA   Noll K.M.;
RT   "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT   the Thermotogales.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP000702; ABQ47017.1; -; Genomic_DNA.
DR   RefSeq; WP_011943554.1; NC_009486.1.
DR   AlphaFoldDB; A5ILE4; -.
DR   STRING; 390874.Tpet_0999; -.
DR   KEGG; tpt:Tpet_0999; -.
DR   eggNOG; COG1368; Bacteria.
DR   HOGENOM; CLU_021310_1_1_0; -.
DR   Proteomes; UP000006558; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd16015; LTA_synthase; 1.
DR   Gene3D; 3.30.1120.170; -; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR012160; LtaS-like.
DR   InterPro; IPR000917; Sulfatase_N.
DR   PANTHER; PTHR47371; LIPOTEICHOIC ACID SYNTHASE; 1.
DR   PANTHER; PTHR47371:SF3; PHOSPHOGLYCEROL TRANSFERASE I; 1.
DR   Pfam; PF00884; Sulfatase; 1.
DR   PIRSF; PIRSF005091; Mmb_sulf_HI1246; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Manganese {ECO:0000256|PIRSR:PIRSR005091-2};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR005091-2};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        27..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        91..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        120..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          202..492
FT                   /note="Sulfatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00884"
FT   ACT_SITE        254
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT   BINDING         210
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         254
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         367
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT   BINDING         427
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         428
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ   SEQUENCE   593 AA;  67553 MW;  C5814442A211825D CRC64;
     MSDYLLIVFL AAKIVLFYVP TLSSFSVSVV FSTAGWLMLL LLVFKGGHKL LYTVLSLLLF
     VDFLYFQNFG NLPSIKEVVL LPQVGDLGGE IKYFIDLYSL LFVADLPFVW FFFKENTKRT
     FSLSSLFVLV LSFTFLGAVH TSQNLQSKFV FNRYGVFDYH VQDIINLFVN KKEENNDLAV
     SSVRSETAEP SQKILFGIGK GKNVIVVQME SLQNFVIGLE VNGQEITPNI NSFLRDSGTV
     YFSNCYQQVG SGNTADAEFV VNTSLHTLGD SVVYEEYPVI NLPALPRIMK QNGYHTIAFH
     GNVGWFWNRE EVYKHIGFDE FVSLEDFQQD EVFGMGLADV SFFKQAVQKL RNYPQPFYAF
     LITISSHTPF VIPEEHRKLE LPEDISDTIV GHYLQAIHYA DEAFGVFLDE LKRAGLYENS
     VIVLYGDHAG LYPFNREVKT KIPEILDREF SFEIALNIPF AIHIPGENIR RVVNIPGGQI
     DFLPTILNVM GINYREGFFM GQDLLNAKHG FAALRYHVPD GSFIDDNRVF IVSWDGRLDK
     SLAVDRKNGT PQRYVEFLDG YVKAIQQIEA SRYFILRNCQ PLQKVAKDQT SSR
//
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