LTAS_STAHJ
ID LTAS_STAHJ Reviewed; 645 AA.
AC Q4L4D7;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Lipoteichoic acid synthase;
DE Contains:
DE RecName: Full=Glycerol phosphate lipoteichoic acid synthase;
DE Short=LTA synthase;
DE EC=2.7.8.-;
DE AltName: Full=Polyglycerol phosphate synthase;
DE Contains:
DE RecName: Full=Processed glycerol phosphate lipoteichoic acid synthase;
GN Name=ltaS; OrderedLocusNames=SH2179;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
CC -!- FUNCTION: Catalyzes the polymerization of lipoteichoic acid (LTA)
CC polyglycerol phosphate, a reaction that presumably uses
CC phosphatidylglycerol (PG) as substrate. Is required for staphylococcal
CC growth and cell division process (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Cell wall biogenesis; lipoteichoic acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Processed glycerol phosphate lipoteichoic acid
CC synthase]: Secreted {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LTA synthase family. {ECO:0000305}.
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DR EMBL; AP006716; BAE05488.1; -; Genomic_DNA.
DR RefSeq; WP_011276440.1; NC_007168.1.
DR AlphaFoldDB; Q4L4D7; -.
DR SMR; Q4L4D7; -.
DR STRING; 279808.SH2179; -.
DR EnsemblBacteria; BAE05488; BAE05488; SH2179.
DR GeneID; 58061697; -.
DR KEGG; sha:SH2179; -.
DR eggNOG; COG1368; Bacteria.
DR HOGENOM; CLU_021310_0_0_9; -.
DR OMA; VSNHRPF; -.
DR OrthoDB; 1067869at2; -.
DR UniPathway; UPA00556; -.
DR Proteomes; UP000000543; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0070395; P:lipoteichoic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR012160; LtaS-like.
DR InterPro; IPR000917; Sulfatase_N.
DR Pfam; PF00884; Sulfatase; 1.
DR PIRSF; PIRSF005091; Mmb_sulf_HI1246; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell wall biogenesis/degradation; Manganese; Membrane;
KW Metal-binding; Secreted; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..217
FT /note="Glycerol phosphate lipoteichoic acid synthase"
FT /id="PRO_0000305372"
FT CHAIN 218..645
FT /note="Processed glycerol phosphate lipoteichoic acid
FT synthase"
FT /id="PRO_0000305373"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..43
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..124
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..645
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 300
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 475
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 476
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT SITE 217..218
FT /note="Cleavage"
FT /evidence="ECO:0000250"
SQ SEQUENCE 645 AA; 74324 MW; 25D1D795E02863A1 CRC64;
MSLHKKKISL FAFFLLTVFT VTLKTYFSYY VDFSLGVKGL VQNLILLMNP YSLIALILSV
FLFFKGKKAY WFIFIGGFLL SFLLYANVVY FRFFSDFLTF STLNQAGNVE SMGGAVGASF
KWYDFVYFID TIVYLFILIF KGSWLDKRVF SKKFVPVVMA ASVALFFLNL AFAETDRPEL
LTRTFDHKYL VKYLGPYNFT VYDGVKTIQN NQQKALASED DLTKVLNYTK QKNTTPNSEY
FGAAKKKNII KIHLESFQTF LINKKVNGKE VTPFLNKLST GNEDFRYYPN FFHQTGQGKT
SDAEFTMDNS LYGLPQGSAY SLKGDNTYQS LPAILDQKQG YTSDVMHGDY KTFWNRDQVY
KHFGIDKFYD ATYYDMSDDN IVNLGLKDKP FFKESAEYQS KMKGPFYSHL ITLTNHYPFT
LSEEDADIDK PNTGDSTVDG YIQTAHYLDQ ALEEYVTDLK KKGLYDDSVI MIYGDHYGIS
ENHNNAMEKL LGEKITPAKF MDLNRTGFWL KIPGKEGTVD KTYAGQMDVM PTILHLVGID
SKNFLMFGTD MLSKDHNDVI PFRNGDFITK DYKYVNGKAY SNKTNELLET QPKDLDKNKK
QVEKDLEMSD NVLNGDLFRF YKNPDFKKID PSKYEYKTGP KGNQK
