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   20-DEC-2017, entry version 117.
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}.
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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   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; HRTSTWQ; -.
DR   PhylomeDB; Q02115; -.
DR   BioCyc; BSUB:BSU35650-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:InterPro.
DR   HAMAP; MF_01140; TagU_transferase; 1.
DR   InterPro; IPR004474; LytR_CpsA_psr.
DR   InterPro; IPR023734; Tscrpt_reg_LytR.
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
//