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LTAS_STAEQ
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   03-AUG-2022, entry version 100.
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; Firmicutes; 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   EnsemblBacteria; AAW53753; AAW53753; SERP0379.
DR   GeneID; 50019355; -.
DR   KEGG; ser:SERP0379; -.
DR   eggNOG; COG1368; Bacteria.
DR   HOGENOM; CLU_021310_0_0_9; -.
DR   OMA; VSNHRPF; -.
DR   OrthoDB; 1067869at2; -.
DR   UniPathway; UPA00556; -.
DR   Proteomes; UP000000531; 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_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
 
 
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