LTAS2_BACSU
ID LTAS2_BACSU Reviewed; 649 AA.
AC O34952; Q79EU0;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Lipoteichoic acid synthase 2;
DE Contains:
DE RecName: Full=Glycerol phosphate lipoteichoic acid synthase 2;
DE Short=LTA synthase 1;
DE EC=2.7.8.-;
DE AltName: Full=Polyglycerol phosphate synthase 2;
DE Contains:
DE RecName: Full=Processed glycerol phosphate lipoteichoic acid synthase 2;
GN Name=ltaS2; Synonyms=yflE; OrderedLocusNames=BSU07710;
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=9272861; DOI=10.1016/s0378-1119(97)00130-3;
RA Yamamoto H., Uchiyama S., Nugroho F.A., Sekiguchi J.;
RT "Cloning and sequencing of a 35.7 kb in the 70 degree-73 degree region of
RT the Bacillus subtilis genome reveal genes for a new two-component system,
RT three spore germination proteins, an iron uptake system and a general
RT stress response protein.";
RL Gene 194:191-199(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 216-226, CLEAVAGE SITE, 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 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 2]: Secreted. Note=The secretion into the extracellular medium
CC is dependent on SecA and Ffh.
CC -!- PTM: Proteolytically cleaved. {ECO:0000269|PubMed:10658653}.
CC -!- MISCELLANEOUS: Restores staphylococcal growth after ltaS depletion.
CC -!- SIMILARITY: Belongs to the LTA synthase family. {ECO:0000305}.
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DR EMBL; D86417; BAA22298.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12600.1; -; Genomic_DNA.
DR PIR; C69810; C69810.
DR RefSeq; NP_388652.1; NC_000964.3.
DR RefSeq; WP_003233694.1; NZ_JNCM01000032.1.
DR PDB; 2W8D; X-ray; 2.35 A; A/B=214-649.
DR PDBsum; 2W8D; -.
DR AlphaFoldDB; O34952; -.
DR SMR; O34952; -.
DR STRING; 224308.BSU07710; -.
DR PaxDb; O34952; -.
DR PRIDE; O34952; -.
DR EnsemblBacteria; CAB12600; CAB12600; BSU_07710.
DR GeneID; 939200; -.
DR KEGG; bsu:BSU07710; -.
DR PATRIC; fig|224308.179.peg.837; -.
DR eggNOG; COG1368; Bacteria.
DR InParanoid; O34952; -.
DR OMA; PLFIHAP; -.
DR PhylomeDB; O34952; -.
DR BioCyc; BSUB:BSU07710-MON; -.
DR UniPathway; UPA00556; -.
DR EvolutionaryTrace; O34952; -.
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 3D-structure; Cell membrane; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Manganese; Membrane; Metal-binding;
KW Reference proteome; Secreted; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..215
FT /note="Glycerol phosphate lipoteichoic acid synthase 2"
FT /id="PRO_0000305348"
FT CHAIN 216..649
FT /note="Processed glycerol phosphate lipoteichoic acid
FT synthase 2"
FT /id="PRO_0000305349"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..42
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..118
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..649
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 622..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 297
FT /evidence="ECO:0000250"
FT BINDING 253
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 412
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 472
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT SITE 215..216
FT /note="Cleavage"
FT HELIX 219..230
FT /evidence="ECO:0007829|PDB:2W8D"
FT TURN 236..244
FT /evidence="ECO:0007829|PDB:2W8D"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:2W8D"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:2W8D"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:2W8D"
FT HELIX 271..278
FT /evidence="ECO:0007829|PDB:2W8D"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:2W8D"
FT STRAND 283..289
FT /evidence="ECO:0007829|PDB:2W8D"
FT HELIX 296..306
FT /evidence="ECO:0007829|PDB:2W8D"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:2W8D"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:2W8D"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:2W8D"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:2W8D"
FT STRAND 338..345
FT /evidence="ECO:0007829|PDB:2W8D"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:2W8D"
FT HELIX 352..358
FT /evidence="ECO:0007829|PDB:2W8D"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:2W8D"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:2W8D"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:2W8D"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:2W8D"
FT HELIX 384..396
FT /evidence="ECO:0007829|PDB:2W8D"
FT STRAND 400..407
FT /evidence="ECO:0007829|PDB:2W8D"
FT HELIX 432..457
FT /evidence="ECO:0007829|PDB:2W8D"
FT STRAND 464..470
FT /evidence="ECO:0007829|PDB:2W8D"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:2W8D"
FT HELIX 480..486
FT /evidence="ECO:0007829|PDB:2W8D"
FT HELIX 494..499
FT /evidence="ECO:0007829|PDB:2W8D"
FT STRAND 505..509
FT /evidence="ECO:0007829|PDB:2W8D"
FT HELIX 523..525
FT /evidence="ECO:0007829|PDB:2W8D"
FT HELIX 526..533
FT /evidence="ECO:0007829|PDB:2W8D"
FT STRAND 567..572
FT /evidence="ECO:0007829|PDB:2W8D"
FT STRAND 575..578
FT /evidence="ECO:0007829|PDB:2W8D"
FT TURN 579..581
FT /evidence="ECO:0007829|PDB:2W8D"
FT HELIX 587..589
FT /evidence="ECO:0007829|PDB:2W8D"
FT HELIX 593..610
FT /evidence="ECO:0007829|PDB:2W8D"
FT HELIX 613..616
FT /evidence="ECO:0007829|PDB:2W8D"
FT HELIX 627..629
FT /evidence="ECO:0007829|PDB:2W8D"
SQ SEQUENCE 649 AA; 74234 MW; D92719F8D3008FBD CRC64;
MKTFIKERGL AFFLIAVVLL WIKTYVGYVL NFNLGIDNTI QKILLFVNPL SSSLFFLGFG
LLFKKKLQQT AIIVIHFLMS FLLYANIVYY RFFNDFITIP VIMQAKTNGG QLGDSAFSLM
RPTDAFYFID TIILIILAIK VNKPAETSSK KSFRIIFASS ILVFLINLAV AESDRPELLT
RSFDRNYLVK YLGTYNFTIY DAVQNIKSNS QRALADSSDV TEVENYMKAN YDVPNNVYFG
KAEGKNVIYV SLESLQSFII DYKIDGKEVT PFLNKLAHDN ETFYFDNFFH QTGQGKTSDA
EFMMENSLYP LAQGSVFVNK AQNTLQSVPA ILKSKNYTSA TFHGNTQTFW NRNEMYKAEG
IDKFFDSAYY DMNEENTKNY GMKDKPFFKE SMPLLESLPQ PFYTKFITLS NHFPFGMDEG
DTDFPAGDFG DSVVDNYFQS AHYLDQSIEQ FFNDLKKDGL YDKSIIVMYG DHYGISENHN
KAMAKVLGKD EITDYDNAQL QRVPLFIHAA GVKGEKVHKY AGDVDVAPTI LHLLGVDTKD
YLMSGSDILS KEHREVIPFR NGDFISPKYT KISGKYYDTK TGKELDESEV DKSEDSLVKK
ELEMSDKIIN GDLLRFYEPK GFKKVNPSDY DYTKHDEDSS ETSKDNEDK
