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 07-NOV-2018, entry version 122. 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, GN ECO:0000303|PubMed:21964069}; GN Synonyms=lytR {ECO:0000303|PubMed:1357079}; GN 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- RT acetylmuramoyl-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., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA 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., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA 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 RT structural gene of UDP-glucose pyrophosphorylase of Bacillus subtilis RT 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) CC from their lipid-linked precursor to the cell wall peptidoglycan CC (PG). {ECO:0000255|HAMAP-Rule:MF_01140, CC 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- CC Rule:MF_01140, ECO:0000305}; Single-pass type II membrane protein CC {ECO:0000255|HAMAP-Rule:MF_01140, ECO:0000305}. CC -!- DISRUPTION PHENOTYPE: Single mutant has no effect on cell growth CC or morphology under normal growth conditions. Triple disruption of CC tagTUV genes is not viable (PubMed:21964069). Cells lacking this CC gene display a considerably increased transcription frequency of CC lytR and lytABC operon expression (PubMed:1357079). CC {ECO:0000269|PubMed:1357079, 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 CC part of a two-component regulatory system that, together with CC LytS, is involved in autolysis and cell wall metabolism. The CC B.subtilis ortholog of S.aureus LytR is LytT (AC P94514). CC {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 ProteinModelPortal; Q02115; -. DR SMR; Q02115; -. DR STRING; 224308.Bsubs1_010100019281; -. 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 HOGENOM; HOG000236372; -. DR InParanoid; Q02115; -. DR OMA; RTSTWQG; -. 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; Complete proteome; KW Membrane; Reference proteome; Signal-anchor; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1 306 Polyisoprenyl-teichoic acid-- FT peptidoglycan teichoic acid transferase FT TagU. FT /FTId=PRO_0000218498. FT TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_01140, ECO:0000305}. FT TRANSMEM 12 32 Helical; Signal-anchor for type II FT membrane protein. {ECO:0000255|HAMAP- FT Rule:MF_01140}. FT TOPO_DOM 33 306 Extracellular. {ECO:0000255|HAMAP- FT Rule:MF_01140, ECO:0000305}. FT MUTAGEN 75 75 D->A: Does not complement the tagTUV FT deletion mutant. FT {ECO:0000269|PubMed:21964069}. FT MUTAGEN 83 83 R->A: Does not complement the tagTUV FT deletion mutant. FT {ECO:0000269|PubMed:21964069}. FT MUTAGEN 85 85 D->A: Does not complement the tagTUV FT deletion mutant. FT {ECO:0000269|PubMed:21964069}. FT MUTAGEN 86 86 T->F: Does not complement the tagTUV FT deletion mutant. FT {ECO:0000269|PubMed:21964069}. FT MUTAGEN 197 197 T->F: Does not complement the tagTUV FT deletion mutant. FT {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 //