LTAS_STAAW
ID LTAS_STAAW Reviewed; 646 AA.
AC Q7A1I3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=MW0681;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 218-641, ALONE AND IN COMPLEX WITH
RP GLYCEROL-PHOSPHATE, ACTIVE SITE, METAL-BINDING SITES, AND MUTAGENESIS OF
RP GLU-255; GLY-298; THR-300; HIS-409; HIS-416; ASP-475 AND HIS-476.
RX PubMed=19168632; DOI=10.1073/pnas.0809020106;
RA Lu D., Wormann M.E., Zhang X., Schneewind O., Grundling A., Freemont P.S.;
RT "Structure-based mechanism of lipoteichoic acid synthesis by Staphylococcus
RT aureus LtaS.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1584-1589(2009).
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; BA000033; BAB94546.1; -; Genomic_DNA.
DR RefSeq; WP_000098285.1; NC_003923.1.
DR PDB; 2W5Q; X-ray; 1.20 A; A=218-641.
DR PDB; 2W5R; X-ray; 1.70 A; A=218-641.
DR PDB; 2W5S; X-ray; 2.10 A; A=218-641.
DR PDB; 2W5T; X-ray; 1.60 A; A=218-641.
DR PDBsum; 2W5Q; -.
DR PDBsum; 2W5R; -.
DR PDBsum; 2W5S; -.
DR PDBsum; 2W5T; -.
DR AlphaFoldDB; Q7A1I3; -.
DR SMR; Q7A1I3; -.
DR EnsemblBacteria; BAB94546; BAB94546; BAB94546.
DR KEGG; sam:MW0681; -.
DR HOGENOM; CLU_021310_0_0_9; -.
DR OMA; VSNHRPF; -.
DR UniPathway; UPA00556; -.
DR EvolutionaryTrace; Q7A1I3; -.
DR Proteomes; UP000000418; 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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell wall biogenesis/degradation; Manganese;
KW Membrane; Metal-binding; Secreted; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..217
FT /note="Glycerol phosphate lipoteichoic acid synthase"
FT /id="PRO_0000305360"
FT CHAIN 218..646
FT /note="Processed glycerol phosphate lipoteichoic acid
FT synthase"
FT /id="PRO_0000305361"
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:0000269|PubMed:19168632"
FT BINDING 255
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 300
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 416
FT /ligand="substrate"
FT BINDING 475
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 476
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT SITE 217..218
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT MUTAGEN 255
FT /note="E->A: No activity."
FT /evidence="ECO:0000269|PubMed:19168632"
FT MUTAGEN 298
FT /note="G->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:19168632"
FT MUTAGEN 300
FT /note="T->A,V: No activity."
FT /evidence="ECO:0000269|PubMed:19168632"
FT MUTAGEN 409
FT /note="H->A: Retained activity."
FT /evidence="ECO:0000269|PubMed:19168632"
FT MUTAGEN 416
FT /note="H->A: No activity."
FT /evidence="ECO:0000269|PubMed:19168632"
FT MUTAGEN 475
FT /note="D->A: No activity."
FT /evidence="ECO:0000269|PubMed:19168632"
FT MUTAGEN 476
FT /note="H->A: No activity."
FT /evidence="ECO:0000269|PubMed:19168632"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:2W5Q"
FT TURN 229..232
FT /evidence="ECO:0007829|PDB:2W5Q"
FT TURN 238..246
FT /evidence="ECO:0007829|PDB:2W5Q"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:2W5Q"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:2W5Q"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:2W5Q"
FT HELIX 273..279
FT /evidence="ECO:0007829|PDB:2W5Q"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:2W5Q"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:2W5Q"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:2W5Q"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:2W5Q"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:2W5Q"
FT HELIX 331..339
FT /evidence="ECO:0007829|PDB:2W5Q"
FT STRAND 342..349
FT /evidence="ECO:0007829|PDB:2W5Q"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:2W5Q"
FT HELIX 356..363
FT /evidence="ECO:0007829|PDB:2W5Q"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:2W5Q"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:2W5Q"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:2W5Q"
FT HELIX 388..400
FT /evidence="ECO:0007829|PDB:2W5Q"
FT STRAND 404..411
FT /evidence="ECO:0007829|PDB:2W5Q"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:2W5Q"
FT HELIX 436..461
FT /evidence="ECO:0007829|PDB:2W5Q"
FT STRAND 468..474
FT /evidence="ECO:0007829|PDB:2W5Q"
FT HELIX 481..483
FT /evidence="ECO:0007829|PDB:2W5Q"
FT HELIX 484..491
FT /evidence="ECO:0007829|PDB:2W5Q"
FT HELIX 497..502
FT /evidence="ECO:0007829|PDB:2W5Q"
FT STRAND 508..511
FT /evidence="ECO:0007829|PDB:2W5Q"
FT HELIX 526..528
FT /evidence="ECO:0007829|PDB:2W5Q"
FT HELIX 529..537
FT /evidence="ECO:0007829|PDB:2W5Q"
FT STRAND 559..561
FT /evidence="ECO:0007829|PDB:2W5Q"
FT STRAND 567..575
FT /evidence="ECO:0007829|PDB:2W5Q"
FT STRAND 578..581
FT /evidence="ECO:0007829|PDB:2W5Q"
FT TURN 582..584
FT /evidence="ECO:0007829|PDB:2W5Q"
FT HELIX 595..615
FT /evidence="ECO:0007829|PDB:2W5Q"
FT HELIX 617..620
FT /evidence="ECO:0007829|PDB:2W5Q"
FT HELIX 631..633
FT /evidence="ECO:0007829|PDB:2W5Q"
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
