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 26-FEB-2020, entry version 127. 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). 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. {ECO:0000269|PubMed:21964069}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01140, CC ECO:0000305}; Single-pass type II membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01140, ECO:0000305}. 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 SMR; Q02115; -. DR STRING; 224308.BSU35650; -. DR jPOST; Q02115; -. DR PaxDb; Q02115; -. DR PRIDE; Q02115; -. DR DNASU; 936787; -. DR EnsemblBacteria; CAB15582; CAB15582; BSU35650. DR GeneID; 936787; -. DR KEGG; bsu:BSU35650; -. DR PATRIC; fig|224308.179.peg.3856; -. DR eggNOG; COG1316; LUCA. DR InParanoid; Q02115; -. DR KO; K01005; -. DR OMA; MGGLVKM; -. DR PhylomeDB; Q02115; -. DR BioCyc; BSUB:BSU35650-MONOMER; -. DR BioCyc; MetaCyc:BSU35650-MONOMER; -. DR Proteomes; UP000001570; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule. 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 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" 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 //