LTAS_STAAB
ID LTAS_STAAB Reviewed; 646 AA.
AC Q2YSL2;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=SAB0668;
OS Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=273036;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bovine RF122 / ET3-1;
RX PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT "Molecular correlates of host specialization in Staphylococcus aureus.";
RL PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI80356.1; -; Genomic_DNA.
DR RefSeq; WP_000098286.1; NC_007622.1.
DR AlphaFoldDB; Q2YSL2; -.
DR SMR; Q2YSL2; -.
DR KEGG; sab:SAB0668; -.
DR HOGENOM; CLU_021310_0_0_9; -.
DR OMA; VSNHRPF; -.
DR UniPathway; UPA00556; -.
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_0000305350"
FT CHAIN 218..646
FT /note="Processed glycerol phosphate lipoteichoic acid
FT synthase"
FT /id="PRO_0000305351"
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..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..119
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..646
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 623..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 646 AA; 74399 MW; 5886236C58EB6C2A CRC64;
MSSQKKKISL FAFFLLTVIT ITLKTYFSYY VDFSLGVKGL VQNLILLMNP YSLVALVLSV
FLFFKGKKAF WFMFIGGFLL TFLLYANVVY FRFFSDFLTF STLNQVGNVE SMGGAVSASF
KWYDFVYFID TLVYLFILIF KTKWLDTKAF SKKFVPVVMA ASVALFFLNL AFAETDRPEL
LTRTFDHKYL VKYLGPYNFT VYDGVKTIEN NQQKALASED DLTKVLNYTK QRQTEPNPEY
YGVAKKKNII KIHLESFQTF LINKKVNGKE VTPFLNKLSS GKQQFTYFPN FFHQTGQGKT
SDSEFTMDNS LYGLPQGSAF SLKGDNTYQS LPAILDQKQG YKSDVMHGDY KTFWNRDQVY
KHFGIDKFYD ATYYDMSDKN VVNLGLKDKI FFKDSANYQA KMKSPFYSHL ITLTNHYPFT
LDEKDATIEK SNTGDATVDG YIQTARYLDE ALEEYINDLK KKGLYDNSVI MIYGDHYGIS
ENHNNAMEKL LGEKITPAKF TDLNRTGFWI KIPGKSGGIN NEYAGQVDVM PTILHLAGID
TKNYLMFGTD LFSKGHNQVV PFRNGDFITK DYKYVNGKIY SNKNNELITT QPADFEKNKK
QVEKDLEMSD NVLNGDLFRF YKNPDFKKVN PSKYKYETGP KANSKK
