ID L0EJG4_THECK Unreviewed; 633 AA.
AC L0EJG4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Phosphoglycerol transferase family protein, alkaline phosphatase superfamily {ECO:0000313|EMBL:AGA59330.1};
GN OrderedLocusNames=Theco_3278 {ECO:0000313|EMBL:AGA59330.1};
OS Thermobacillus composti (strain DSM 18247 / JCM 13945 / KWC4).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Thermobacillus.
OX NCBI_TaxID=717605 {ECO:0000313|EMBL:AGA59330.1, ECO:0000313|Proteomes:UP000010795};
RN [1] {ECO:0000313|Proteomes:UP000010795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18247 / JCM 13945 / KWC4
RC {ECO:0000313|Proteomes:UP000010795};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Anderson I.,
RA Woyke T.;
RT "Complete sequence of chromosome of Thermobacillus composti KWC4.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|PIRNR:PIRNR005091}.
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DR EMBL; CP003255; AGA59330.1; -; Genomic_DNA.
DR RefSeq; WP_015256062.1; NC_019897.1.
DR AlphaFoldDB; L0EJG4; -.
DR STRING; 717605.Theco_3278; -.
DR KEGG; tco:Theco_3278; -.
DR eggNOG; COG1368; Bacteria.
DR HOGENOM; CLU_021310_1_1_9; -.
DR OrthoDB; 5901192at2; -.
DR Proteomes; UP000010795; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; 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 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR005091};
KW Manganese {ECO:0000256|PIRSR:PIRSR005091-2};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR005091};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR005091-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000010795};
KW Transferase {ECO:0000313|EMBL:AGA59330.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 236..528
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT ACT_SITE 285
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT BINDING 243
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 285
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 401
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT BINDING 461
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 462
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ SEQUENCE 633 AA; 70958 MW; 7CE156063ABC5060 CRC64;
MNERVREALR SPFAVFTVLL TIKFYMASSV VFDGSVWNPL ITSLPSVWAA FALIELLTDK
RKTLAYAIVD LIYTCVYFAV IMYYKYFGII VTYHAFSQIG QVKEVKGSVF QLMHPYFLLI
FADLVVIALL AARHRGFRRW ASRPRPSRAY RMGAAVLFLV MFVICALQVV PNRGIVNELA
RAERMGIINY EVDIMLTSRR EALHEPSVVT PAAVREVKRL PQTGVPAYWS AAGGRHVIFI
QLEAFQTILL DLKVDGVEVT PVLNRLKEEG VYFPRFFQQV GAGNTSDAEY TANTSLLTPP
AGAASETYGR KALPSLPKLL HARGYETVTF HTNDVKFWHR DALYPALGFD RYYDQQFFRD
EDFVHFGSSD EVLYRKSVAE LKALADEGQK VYANLISMSA HHPFNLPAHK DTFDLPERFR
GTFVGDYLRS QHYADKALGL FIEEMKAAGL WENSLIVIYG DHMGMPVYSL TKEDRSLLKE
LLGRTYGYYD MLRVPLLIVA PGALEPQTIE AVGGHTDIMP TVANLAGVRL DGSVVFGQDL
LNYRSNLLPI RYYLPTGSFI NDHAIFVPGE GFGDGTVYPL DGGKPGGADS VGADGAPLVT
EDEYRRALDL FRMSHSYISQ LPERPKEGGR QSS
//
