TAGU_BACSU
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 03-AUG-2022, entry version 136.
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 PRIDE; 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-MON; -.
DR BioCyc; MetaCyc:BSU35650-MON; -.
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
