LTAS1_BACSU
ID LTAS1_BACSU Reviewed; 639 AA.
AC Q797B3; O06487;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Lipoteichoic acid synthase 1;
DE Contains:
DE RecName: Full=Glycerol phosphate lipoteichoic acid synthase 1;
DE Short=LTA synthase 1;
DE EC=2.7.8.-;
DE AltName: Full=Polyglycerol phosphate synthase 1;
DE Contains:
DE RecName: Full=Processed glycerol phosphate lipoteichoic acid synthase 1;
GN Name=ltaS1; Synonyms=yfnI; OrderedLocusNames=BSU07260;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / AC327;
RX PubMed=9141694; DOI=10.1099/00221287-143-4-1317;
RA Yamamoto H., Uchiyama S., Nugroho F.A., Sekiguchi J.;
RT "A 23.4 kb segment at the 69 degrees-70 degrees region of the Bacillus
RT subtilis genome.";
RL Microbiology 143:1317-1320(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP PROTEIN SEQUENCE OF 215-229, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=10658653; DOI=10.1099/00221287-146-1-65;
RA Hirose I., Sano K., Shioda I., Kumano M., Nakamura K., Yamane K.;
RT "Proteome analysis of Bacillus subtilis extracellular proteins: a two-
RT dimensional protein electrophoretic study.";
RL Microbiology 146:65-75(2000).
RN [4]
RP PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP PROCESSING BY SIPT/SIPV.
RC STRAIN=168;
RX PubMed=11544192; DOI=10.1101/gr.182801;
RA Antelmann H., Tjalsma H., Voigt B., Ohlmeier S., Bron S., van Dijl J.M.,
RA Hecker M.;
RT "A proteomic view on genome-based signal peptide predictions.";
RL Genome Res. 11:1484-1502(2001).
RN [5]
RP INDUCTION.
RC STRAIN=168 / 1604;
RX PubMed=17434969; DOI=10.1128/jb.00130-07;
RA Jervis A.J., Thackray P.D., Houston C.W., Horsburgh M.J., Moir A.;
RT "SigM-responsive genes of Bacillus subtilis and their promoters.";
RL J. Bacteriol. 189:4534-4538(2007).
RN [6]
RP FUNCTION IN LTA BIOSYNTHESIS.
RC STRAIN=168;
RX PubMed=17483484; DOI=10.1073/pnas.0701821104;
RA Gruendling A., Schneewind O.;
RT "Synthesis of glycerol phosphate lipoteichoic acid in Staphylococcus
RT aureus.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8478-8483(2007).
CC -!- FUNCTION: Catalyzes the polymerization of lipoteichoic acid (LTA)
CC polyglycerol phosphate, a reaction that presumably uses
CC phosphatidylglycerol (PG) as substrate. {ECO:0000269|PubMed:17483484}.
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 1]: Secreted. Note=The secretion into the extracellular medium
CC is dependent on SecA and Ffh.
CC -!- INDUCTION: Transcribed under partial control of SigM ECF sigma factor
CC (PubMed:17434969). {ECO:0000269|PubMed:17434969}.
CC -!- PTM: Proteolytically cleaved by the type I signal peptidases SipT and
CC SipV.
CC -!- MISCELLANEOUS: Could not restore staphylococcal growth after ltaS
CC depletion.
CC -!- SIMILARITY: Belongs to the LTA synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20118.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D86418; BAA20118.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB12545.2; -; Genomic_DNA.
DR PIR; D69815; D69815.
DR RefSeq; NP_388607.2; NC_000964.3.
DR RefSeq; WP_003243930.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; Q797B3; -.
DR SMR; Q797B3; -.
DR STRING; 224308.BSU07260; -.
DR PaxDb; Q797B3; -.
DR PRIDE; Q797B3; -.
DR EnsemblBacteria; CAB12545; CAB12545; BSU_07260.
DR GeneID; 936099; -.
DR KEGG; bsu:BSU07260; -.
DR PATRIC; fig|224308.179.peg.788; -.
DR eggNOG; COG1368; Bacteria.
DR InParanoid; Q797B3; -.
DR OMA; VSNHRPF; -.
DR PhylomeDB; Q797B3; -.
DR BioCyc; BSUB:BSU07260-MON; -.
DR UniPathway; UPA00556; -.
DR Proteomes; UP000001570; 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 Cell membrane; Cell wall biogenesis/degradation; Direct protein sequencing;
KW Manganese; Membrane; Metal-binding; Reference proteome; Secreted;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..214
FT /note="Glycerol phosphate lipoteichoic acid synthase 1"
FT /id="PRO_0000305346"
FT CHAIN 215..639
FT /note="Processed glycerol phosphate lipoteichoic acid
FT synthase 1"
FT /id="PRO_0000305347"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..41
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..639
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 297
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 413
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 472
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 473
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT SITE 214..215
FT /note="Cleavage; by SipT/SipV"
SQ SEQUENCE 639 AA; 73315 MW; 6761DC69CB366CE6 CRC64;
MKKLFSYKLS FFVLAVILFW AKTYLSYKTE FNLGVKGTTQ EILLIFNPFS SAVFFLGLAL
LAKGRKSAII MLIIDFLMTF VLYANILFYR FFDDFLTFPN IKQSGNVGNM GDGIFSIMAG
HDIFYFLDII ILIAVLIWRP ELKEYKMKKR FASLVILSGI ALFFINLHYA EKDRPQLLTR
TFDRNYIVKY LGLYNYTIYD GVQTAQTETQ RAYASSDDLT SVENYTTSHY AKPNAEYFGS
AKGKNIIKIH LESFQSFLID YKLNGEEVTP FLNKLAHGGE DVTYFDNFFH QTGQGKTSDA
ELTMDNSIFG LPEGSAFVTK GENTYQSLPA ILDQKEGYTS AVLHGDYKSF WNRDQIYKHI
GYDKFFDAST YDMSDENVIN MGLKDKPFFT ESIPKLESLK QPFYAHLITL TNHYPFNLDE
KDASLKKATT GDNTVDSYFQ TARYLDEALE QFFKELKEAG LYDNSVIMIY GDHNGISENH
NRAMKEILGK EITDYQNAQN QRVPLMIRVP GKKGGVNHTY GGEIDVMPTL LHLEGIDSQK
YINFGTDLFS KDHDDTVAFR NGDFVTPKYT SVDNIIYDTK TGEKLKANEE TKNLKTRVNQ
QLSLSDSVLY KDLLRFHKLN DFKAVDPSDY HYGKEKEIK
