ID   LTAS_STAAM              Reviewed;         646 AA.
AC   Q99VQ4;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=SAV0719;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000017; BAB56881.1; -; Genomic_DNA.
DR   RefSeq; WP_000098285.1; NC_002758.2.
DR   AlphaFoldDB; Q99VQ4; -.
DR   SMR; Q99VQ4; -.
DR   World-2DPAGE; 0002:Q99VQ4; -.
DR   PaxDb; Q99VQ4; -.
DR   EnsemblBacteria; BAB56881; BAB56881; SAV0719.
DR   KEGG; sav:SAV0719; -.
DR   HOGENOM; CLU_021310_0_0_9; -.
DR   OMA; VSNHRPF; -.
DR   PhylomeDB; Q99VQ4; -.
DR   BioCyc; SAUR158878:SAV_RS03940-MON; -.
DR   UniPathway; UPA00556; -.
DR   PRO; PR:Q99VQ4; -.
DR   Proteomes; UP000002481; 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_0000305358"
FT   CHAIN           218..646
FT                   /note="Processed glycerol phosphate lipoteichoic acid
FT                   synthase"
FT                   /id="PRO_0000305359"
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