ID LTAS_STAEQ Reviewed; 646 AA.
AC Q5HR16;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 105.
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=SERP0379;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(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; CP000029; AAW53753.1; -; Genomic_DNA.
DR RefSeq; WP_001830354.1; NC_002976.3.
DR AlphaFoldDB; Q5HR16; -.
DR SMR; Q5HR16; -.
DR STRING; 176279.SERP0379; -.
DR GeneID; 50019355; -.
DR KEGG; ser:SERP0379; -.
DR eggNOG; COG1368; Bacteria.
DR HOGENOM; CLU_021310_0_0_9; -.
DR UniPathway; UPA00556; -.
DR Proteomes; UP000000531; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 CDD; cd16015; LTA_synthase; 1.
DR Gene3D; 3.30.1120.170; -; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR012160; LtaS-like.
DR InterPro; IPR000917; Sulfatase_N.
DR PANTHER; PTHR47371; LIPOTEICHOIC ACID SYNTHASE; 1.
DR PANTHER; PTHR47371:SF3; PHOSPHOGLYCEROL TRANSFERASE I; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR PIRSF; PIRSF005091; Mmb_sulf_HI1246; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 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_0000305370"
FT CHAIN 218..646
FT /note="Processed glycerol phosphate lipoteichoic acid
FT synthase"
FT /id="PRO_0000305371"
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 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; 74437 MW; 17A7DA92B801AB1B CRC64;
MSLPKKKIGI FAFFLLTVFT ITLKTYFSYY VDFSLGVKGL VQNLILLMNP YSLIALVLSV
FLFFKGKKAF WFIFIGGFLL TFLLYANVVY FRFFSDFLTF STLNQAGNVE SMGGAVSASF
KWYDFVYFID TIIYLAILIF KRKWLDNRAF SKKFVPVVMA TSVALFFLNL AFAETDRPEL
LTRTFDHKYL VKYLGPYNFT VYDGVKTIEN NQQKALASED DLTKVLNYTK QKRTEPNPEY
YGAAKKKNII KIHLESFQTF LINKKVNGKE VTPFLNKLSS GNQDFTYFPN FFHQTGQGKT
SDSEFTMDNS LYGLPQGSAY SLKGDNTYQS LPAILDQKQG YTSNVMHGDY KTFWNRDQVY
KHFGIDNFYD ATYYDMSDDN IVNLGLKDKP FFKASADYQS KMKKPFYSHL ITLTNHYPFT
LDEEDASIDK PNTGDSTVDG YIQTAHYLDQ ALEEYITDLK KKGLYDNSVI MIYGDHYGIS
ENHNNAMEKL LGEKITPAKF TDLNRTGFWL KVPGKSGGVN KEYAGQMDVM PTLLHLVGID
SKNYLMFGSD MFSKQHNNVV PFRNGDFITE DYKYVNGKIY SNKDNELLTE KPKDFDKNKK
QVEKDLEMSD SVLNGDLFRF YKNPDFKKVN PGKYEYKSGP KGNEKK
//
