ID TAGU_BACSU Reviewed; 306 AA. AC Q02115; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 25-MAY-2022, entry version 135. DE RecName: Full=Polyisoprenyl-teichoic acid--peptidoglycan teichoic acid transferase TagU {ECO:0000255|HAMAP-Rule:MF_01140, ECO:0000305}; DE EC=2.7.8.- {ECO:0000255|HAMAP-Rule:MF_01140, ECO:0000269|PubMed:21964069}; DE AltName: Full=Membrane-bound protein LytR; GN Name=tagU {ECO:0000255|HAMAP-Rule:MF_01140, ECO:0000303|PubMed:21964069}; GN Synonyms=lytR {ECO:0000303|PubMed:1357079}; OrderedLocusNames=BSU35650; OS Bacillus subtilis (strain 168). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE. RC STRAIN=168; RX PubMed=1357079; DOI=10.1099/00221287-138-9-1949; RA Lazarevic V., Margot P., Soldo B., Karamata D.; RT "Sequencing and analysis of the Bacillus subtilis lytRABC divergon: a RT regulatory unit encompassing the structural genes of the N-acetylmuramoyl- RT L-alanine amidase and its modifier."; RL J. Gen. Microbiol. 138:1949-1961(1992). 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 257-306. RC STRAIN=168; RX PubMed=8126437; DOI=10.1099/00221287-139-12-3185; RA Soldo B., Lazarevic V., Margot P., Karamata D.; RT "Sequencing and analysis of the divergon comprising gtaB, the structural RT gene of UDP-glucose pyrophosphorylase of Bacillus subtilis 168."; RL J. Gen. Microbiol. 139:3185-3195(1993). RN [4] RP FUNCTION, PATHWAY, INTERACTION WITH MREB, DISRUPTION PHENOTYPE, AND RP MUTAGENESIS OF ASP-75; ARG-83; ASP-85; THR-86 AND THR-197. RX PubMed=21964069; DOI=10.1038/emboj.2011.358; RA Kawai Y., Marles-Wright J., Cleverley R.M., Emmins R., Ishikawa S., RA Kuwano M., Heinz N., Bui N.K., Hoyland C.N., Ogasawara N., Lewis R.J., RA Vollmer W., Daniel R.A., Errington J.; RT "A widespread family of bacterial cell wall assembly proteins."; RL EMBO J. 30:4931-4941(2011). RN [5] RP INTERACTION WITH FLOT, AND SUBCELLULAR LOCATION. RC STRAIN=168; RX PubMed=23651456; DOI=10.1111/mmi.12252; RA Bach J.N., Bramkamp M.; RT "Flotillins functionally organize the bacterial membrane."; RL Mol. Microbiol. 88:1205-1217(2013). CC -!- FUNCTION: May catalyze the final step in cell wall teichoic acid CC biosynthesis, the transfer of the anionic cell wall polymers (APs) from CC their lipid-linked precursor to the cell wall peptidoglycan (PG). CC {ECO:0000255|HAMAP-Rule:MF_01140, ECO:0000269|PubMed:21964069}. CC -!- PATHWAY: Cell wall biogenesis. {ECO:0000255|HAMAP-Rule:MF_01140, CC ECO:0000269|PubMed:21964069}. CC -!- SUBUNIT: Interacts with MreB (PubMed:21964069). Interacts with FloT CC (PubMed:23651456). {ECO:0000269|PubMed:21964069, CC ECO:0000269|PubMed:23651456}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01140, CC ECO:0000269|PubMed:23651456, ECO:0000305}; Single-pass type II membrane CC protein {ECO:0000255|HAMAP-Rule:MF_01140, ECO:0000305}. Membrane raft CC {ECO:0000269|PubMed:23651456}; Single-pass type II membrane protein. CC Note=Present in detergent-resistant membrane (DRM) fractions that may CC be equivalent to eukaryotic membrane rafts; these rafts include CC proteins involved in signaling, molecule trafficking and protein CC secretion. {ECO:0000269|PubMed:23651456}. CC -!- DISRUPTION PHENOTYPE: Single mutant has no effect on cell growth or CC morphology under normal growth conditions. Triple disruption of tagTUV CC genes is not viable (PubMed:21964069). Cells lacking this gene display CC a considerably increased transcription frequency of lytR and lytABC CC operon expression (PubMed:1357079). {ECO:0000269|PubMed:1357079, CC ECO:0000269|PubMed:21964069}. CC -!- SIMILARITY: Belongs to the LytR/CpsA/Psr (LCP) family. CC {ECO:0000255|HAMAP-Rule:MF_01140, ECO:0000305}. CC -!- CAUTION: Was originally thought to be involved in transcriptional CC regulation. {ECO:0000305|PubMed:1357079}. CC -!- CAUTION: This protein is unrelated to LytR from S.aureus, which is part CC of a two-component regulatory system that, together with LytS, is CC involved in autolysis and cell wall metabolism. The B.subtilis ortholog CC of S.aureus LytR is LytT (AC P94514). {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M87645; AAA22578.1; -; Genomic_DNA. DR EMBL; AL009126; CAB15582.1; -; Genomic_DNA. DR EMBL; Z22516; CAA80239.1; -; Genomic_DNA. DR PIR; A47679; A47679. DR RefSeq; NP_391445.1; NC_000964.3. DR RefSeq; WP_003227949.1; NZ_JNCM01000033.1. DR PDB; 6UF6; X-ray; 2.20 A; A=61-306. DR PDBsum; 6UF6; -. DR AlphaFoldDB; Q02115; -. DR SMR; Q02115; -. DR STRING; 224308.BSU35650; -. DR jPOST; Q02115; -. DR PaxDb; Q02115; -. DR DNASU; 936787; -. DR EnsemblBacteria; CAB15582; CAB15582; BSU_35650. DR GeneID; 936787; -. DR KEGG; bsu:BSU35650; -. DR PATRIC; fig|224308.179.peg.3856; -. DR eggNOG; COG1316; Bacteria. DR InParanoid; Q02115; -. DR OMA; LLGYKDC; -. DR PhylomeDB; Q02115; -. DR BioCyc; BSUB:BSU35650-MONOMER; -. DR Proteomes; UP000001570; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule. DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:UniProtKB-UniRule. DR GO; GO:0070726; P:cell wall assembly; IEA:UniProtKB-UniRule. DR HAMAP; MF_01140; TagU_transferase; 1. DR InterPro; IPR004474; LytR_CpsA_psr. DR InterPro; IPR023734; TagU. DR Pfam; PF03816; LytR_cpsA_psr; 1. DR TIGRFAMs; TIGR00350; lytR_cpsA_psr; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Cell wall biogenesis/degradation; Membrane; KW Reference proteome; Signal-anchor; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1..306 FT /note="Polyisoprenyl-teichoic acid--peptidoglycan teichoic FT acid transferase TagU" FT /id="PRO_0000218498" FT TOPO_DOM 1..11 FT /note="Cytoplasmic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01140, ECO:0000305" FT TRANSMEM 12..32 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01140" FT TOPO_DOM 33..306 FT /note="Extracellular" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01140, ECO:0000305" FT MUTAGEN 75 FT /note="D->A: Does not complement the tagTUV deletion FT mutant." FT /evidence="ECO:0000269|PubMed:21964069" FT MUTAGEN 83 FT /note="R->A: Does not complement the tagTUV deletion FT mutant." FT /evidence="ECO:0000269|PubMed:21964069" FT MUTAGEN 85 FT /note="D->A: Does not complement the tagTUV deletion FT mutant." FT /evidence="ECO:0000269|PubMed:21964069" FT MUTAGEN 86 FT /note="T->F: Does not complement the tagTUV deletion FT mutant." FT /evidence="ECO:0000269|PubMed:21964069" FT MUTAGEN 197 FT /note="T->F: Does not complement the tagTUV deletion FT mutant." FT /evidence="ECO:0000269|PubMed:21964069" FT STRAND 67..74 FT /evidence="ECO:0007829|PDB:6UF6" FT STRAND 86..93 FT /evidence="ECO:0007829|PDB:6UF6" FT TURN 94..97 FT /evidence="ECO:0007829|PDB:6UF6" FT STRAND 98..104 FT /evidence="ECO:0007829|PDB:6UF6" FT STRAND 108..112 FT /evidence="ECO:0007829|PDB:6UF6" FT TURN 113..116 FT /evidence="ECO:0007829|PDB:6UF6" FT STRAND 117..120 FT /evidence="ECO:0007829|PDB:6UF6" FT HELIX 121..123 FT /evidence="ECO:0007829|PDB:6UF6" FT HELIX 124..141 FT /evidence="ECO:0007829|PDB:6UF6" FT STRAND 147..152 FT /evidence="ECO:0007829|PDB:6UF6" FT HELIX 153..155 FT /evidence="ECO:0007829|PDB:6UF6" FT HELIX 156..162 FT /evidence="ECO:0007829|PDB:6UF6" FT STRAND 166..172 FT /evidence="ECO:0007829|PDB:6UF6" FT STRAND 174..176 FT /evidence="ECO:0007829|PDB:6UF6" FT STRAND 179..181 FT /evidence="ECO:0007829|PDB:6UF6" FT STRAND 183..188 FT /evidence="ECO:0007829|PDB:6UF6" FT HELIX 190..198 FT /evidence="ECO:0007829|PDB:6UF6" FT TURN 204..206 FT /evidence="ECO:0007829|PDB:6UF6" FT HELIX 207..226 FT /evidence="ECO:0007829|PDB:6UF6" FT HELIX 231..241 FT /evidence="ECO:0007829|PDB:6UF6" FT TURN 242..244 FT /evidence="ECO:0007829|PDB:6UF6" FT STRAND 245..247 FT /evidence="ECO:0007829|PDB:6UF6" FT HELIX 251..256 FT /evidence="ECO:0007829|PDB:6UF6" FT STRAND 268..271 FT /evidence="ECO:0007829|PDB:6UF6" FT STRAND 275..279 FT /evidence="ECO:0007829|PDB:6UF6" FT STRAND 284..288 FT /evidence="ECO:0007829|PDB:6UF6" FT HELIX 290..304 FT /evidence="ECO:0007829|PDB:6UF6" SQ SEQUENCE 306 AA; 34586 MW; E79BE5DDFFA3B089 CRC64; MRNERRKKKK TLLLTILTII GLLVLGTGGY AYYLWHKAAS TVASIHESID KSKKRDKEVS INKKDPFSVL IMGVDERDGD KGRADTLIYM TVNPKTNTTD MVSIPRDTYT KIIGKGTMDK INHSYAFGGT QMTVDTVENF LDVPVDYFVK VNMESFRDVV DTLGGITVNS TFAFSYDGYS FGKGEITLNG KEALAYTRMR KEDPRGDFGR QDRQRQVIQG IINKGANISS ITKFGDMFKV VENNVKTNLT FDNMWDIQSD YKGARKHIKQ HELKGTGTKI NGIYYYQADE SALSDITKEL KESLEK //