LTAS_STAAS
ID LTAS_STAAS Reviewed; 646 AA.
AC Q6GBB1;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=SAS0684;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571857; CAG42460.1; -; Genomic_DNA.
DR RefSeq; WP_000098285.1; NC_002953.3.
DR AlphaFoldDB; Q6GBB1; -.
DR SMR; Q6GBB1; -.
DR KEGG; sas:SAS0684; -.
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_0000305356"
FT CHAIN 218..646
FT /note="Processed glycerol phosphate lipoteichoic acid
FT synthase"
FT /id="PRO_0000305357"
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; 74400 MW; 788FE36EB4528BB0 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 GKEQFTYFPN 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
