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   17-JUN-2020, entry version 128.
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}.
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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   PDB; 6UF6; X-ray; 2.20 A; A=61-306.
DR   PDBsum; 6UF6; -.
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; 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   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"
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
//