LTAS_STAS1
ID LTAS_STAS1 Reviewed; 646 AA.
AC Q49VR4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=SSP2001;
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE19146.1; -; Genomic_DNA.
DR RefSeq; WP_011303659.1; NZ_MTGA01000039.1.
DR AlphaFoldDB; Q49VR4; -.
DR SMR; Q49VR4; -.
DR STRING; 342451.SSP2001; -.
DR EnsemblBacteria; BAE19146; BAE19146; SSP2001.
DR KEGG; ssp:SSP2001; -.
DR PATRIC; fig|342451.11.peg.1995; -.
DR eggNOG; COG1368; Bacteria.
DR HOGENOM; CLU_021310_0_0_9; -.
DR OMA; VSNHRPF; -.
DR OrthoDB; 1067869at2; -.
DR UniPathway; UPA00556; -.
DR Proteomes; UP000006371; 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; Reference proteome; Secreted; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..217
FT /note="Glycerol phosphate lipoteichoic acid synthase"
FT /id="PRO_0000305374"
FT CHAIN 218..646
FT /note="Processed glycerol phosphate lipoteichoic acid
FT synthase"
FT /id="PRO_0000305375"
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 579..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..646
FT /note="Basic and acidic residues"
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; 74912 MW; 265D21B8C60B02A8 CRC64;
MKLHKKKLTL FAFFILTVLT VTLKTYFSYY VDFSLGVKGL VQNLILLMNP YSLIALVLSI
FLFFKGKKAF WFIFIGGFIL TFLLYANVVY FRFFSDFLTF STLNQAGNVE SMGGAVTASF
KWYDFVYFID TIIYLFVLIF KQKWLDKRVF SKKFVPVVMA ASIALFFLNL AFAESDRPEL
LTRTFDHKYL VKYLGPYNFT VYDGVKTIQN NQQKALANED DLTKVLNYTK QKQTEPNKEY
FGAAKKKNII KIHLESFQTF LINKKVNGEE VTPFLNKLST GNEGYRYYPN FYHQTGQGKT
SDSEFTMDNS LFGLPQGSAY SLKGDNTYQS LPAILDQQQG YTSSVMHGDY KTFWNRDQVY
KHFGIDKFYD ATYYDMSEDN IENLGLKDKE FFKESADYLA KEKQPFYNHL ITLTNHYPFT
VSPEDASIEK PNTGDSTVDG YIQTARYLDE SLEEFVNELK KKGLYDDSVI MIYGDHYGIS
ENHNKAMEKL LGEDITPAKF NDLNRTGFWL KIPGKEGTVD KTYAGQADVM PTILHLMGID
TKNYLMMGTD LLSKDHNDTV PFRNGDFVTK DYKYVNGRIY DNKNNEPMTE KPKDFEKRKQ
QSEKDLQMSD DVLNGDLLRF YDNPDFDKIK PSEYEYKTGP KGQERK
