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Database: UniProt
Entry: I6TBV1_ENTHA
LinkDB: I6TBV1_ENTHA
Original site: I6TBV1_ENTHA 
ID   I6TBV1_ENTHA            Unreviewed;       713 AA.
AC   I6TBV1;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Sulfatase domain-containing protein {ECO:0000313|EMBL:AFM70849.1};
GN   OrderedLocusNames=EHR_09720 {ECO:0000313|EMBL:AFM70849.1};
OS   Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 /
OS   NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=768486 {ECO:0000313|EMBL:AFM70849.1, ECO:0000313|Proteomes:UP000002895};
RN   [1] {ECO:0000313|EMBL:AFM70849.1, ECO:0000313|Proteomes:UP000002895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB
RC   6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R
RC   {ECO:0000313|Proteomes:UP000002895};
RX   PubMed=22933757; DOI=10.1128/JB.01075-12;
RA   Gaechter T., Wunderlin C., Schmidheini T., Solioz M.;
RT   "Genome sequence of Enterococcus hirae (Streptococcus faecalis) ATCC 9790,
RT   a model organism for the study of ion transport, bioenergetics, and copper
RT   homeostasis.";
RL   J. Bacteriol. 194:5126-5127(2012).
CC   -!- PATHWAY: Cell wall biogenesis; lipoteichoic acid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004936}.
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}.
CC   -!- SIMILARITY: Belongs to the LTA synthase family.
CC       {ECO:0000256|ARBA:ARBA00009983}.
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DR   EMBL; CP003504; AFM70849.1; -; Genomic_DNA.
DR   RefSeq; WP_010737847.1; NZ_KB946231.1.
DR   AlphaFoldDB; I6TBV1; -.
DR   KEGG; ehr:EHR_09720; -.
DR   PATRIC; fig|768486.10.peg.1703; -.
DR   eggNOG; COG1368; Bacteria.
DR   HOGENOM; CLU_021310_0_0_9; -.
DR   OrthoDB; 5901192at2; -.
DR   Proteomes; UP000002895; 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; 2.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   3: Inferred from homology;
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   Reference proteome {ECO:0000313|Proteomes:UP000002895};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        74..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        130..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        160..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          252..554
FT                   /note="Sulfatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00884"
FT   REGION          668..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        673..713
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        309
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT   BINDING         260
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         309
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         426
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT   BINDING         486
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         487
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ   SEQUENCE   713 AA;  81058 MW;  D7F5F8C475BADFA8 CRC64;
     MRRIKTPAFL NKRLGFFSLL AVLLWLKTIF AYLFDFNLGI ESGIQYFILF INPIATTLLL
     MGIALYVRRT KASYITMMVI YFLLTLLVFS NVTYYREFTD FITINTILGA GKVASGLGES
     AIRLFRPYDV LYWIDFIIVA ALLITKKIKM DPQPIRARMA FAISTLSVMI FSGNLFLAEA
     DRPELLTRTF SRDYLVKYLG INAFTVYDGI QTYQTNQVRA EASPNDLKEV ESYIKDHYAE
     PNDETFGIAK GKNVIYIHLE SFQQFLIDYK LKDANGVEHE VTPFLNSLYH SNSTFSFDNF
     FHQVKAGKTS DAETLFENSL FGLNQGSLFT QLGGKNTFQA APDILSQTQG YTSAAFHGNA
     GTFWNRNETY KKLGYNYFFD ASYYDVNDDN SFQYGLHDKP FFQQSVQYLE HLQQPFYSKF
     IAVSNHYPYS KFTNEEAGFP LATTNDETIN GYFATANYLD TAVEEFFNYL KVSGLYDNSV
     IVLYGDHYGI SNSRNKSLAE LVGKTSDTWT NFDNAQMQRV PYMIHLPGQT NGGINHTYGG
     QVDALPTLLH LLGVDTKNYN QLGQDLFSKQ HDQLVTFRDG DFITPKYTYY GGTIYDNKTG
     QAITEPTQEV QNEIDALKEK ANKQLAVSDQ INNGDLLRFS TDTGLDPIEA SQFDYKNGMK
     QLLEKEKELG DKSTSVFSQN NNQSTKDLYE TKTYQQINGT QTSDSVPSSE SDK
//
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