TAGT_BACSU
ID TAGT_BACSU Reviewed; 322 AA.
AC Q7WY78;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Polyisoprenyl-teichoic acid--peptidoglycan teichoic acid transferase TagT {ECO:0000305};
DE EC=2.7.8.- {ECO:0000269|PubMed:21964069};
GN Name=tagT {ECO:0000303|PubMed:21964069}; Synonyms=ywtF;
GN OrderedLocusNames=BSU35840;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP SEQUENCE REVISION.
RX PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA Medigue C., Rose M., Viari A., Danchin A.;
RT "Detecting and analyzing DNA sequencing errors: toward a higher quality of
RT the Bacillus subtilis genome sequence.";
RL Genome Res. 9:1116-1127(1999).
RN [3]
RP SEQUENCE REVISION TO 226.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP FUNCTION, PATHWAY, INTERACTION WITH MREB, AND DISRUPTION PHENOTYPE.
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] {ECO:0007744|PDB:3MEJ}
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 46-322.
RA Kuzin A., Su M., Seetharaman J., Mao M., Xiao R., Ciccosanti C., Lee D.,
RA Everett J.K., Nair R., Acton T.B., Rost B., Montelione G.T., Hunt J.F.,
RA Tong L.;
RT "Northeast structural genomics consortium target SR736.";
RL Submitted (MAR-2010) to the PDB data bank.
RN [6] {ECO:0007744|PDB:4DE9}
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 46-322 IN COMPLEX WITH OCTAPRENYL
RP PYROPHOSPHATE LIPID.
RC STRAIN=168;
RX PubMed=22432711; DOI=10.1089/mdr.2011.0232;
RA Eberhardt A., Hoyland C.N., Vollmer D., Bisle S., Cleverley R.M.,
RA Johnsborg O., Havarstein L.S., Lewis R.J., Vollmer W.;
RT "Attachment of capsular polysaccharide to the cell wall in Streptococcus
RT pneumoniae.";
RL Microb. Drug Resist. 18:240-255(2012).
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:0000269|PubMed:21964069}.
CC -!- PATHWAY: Cell wall biogenesis. {ECO:0000269|PubMed:21964069}.
CC -!- SUBUNIT: Interacts with MreB. {ECO:0000269|PubMed:21964069}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000255, 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. {ECO:0000269|PubMed:21964069}.
CC -!- SIMILARITY: Belongs to the LytR/CpsA/Psr (LCP) family. {ECO:0000305}.
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DR EMBL; AL009126; CAB15601.3; -; Genomic_DNA.
DR RefSeq; NP_391465.2; NC_000964.3.
DR RefSeq; WP_003243404.1; NZ_JNCM01000034.1.
DR PDB; 3MEJ; X-ray; 2.49 A; A=46-322.
DR PDB; 4DE9; X-ray; 1.79 A; A=46-322.
DR PDB; 6MPS; X-ray; 1.86 A; A=46-322.
DR PDB; 6MPT; X-ray; 1.65 A; A=46-322.
DR PDB; 6UF5; X-ray; 2.80 A; A=46-322.
DR PDBsum; 3MEJ; -.
DR PDBsum; 4DE9; -.
DR PDBsum; 6MPS; -.
DR PDBsum; 6MPT; -.
DR PDBsum; 6UF5; -.
DR AlphaFoldDB; Q7WY78; -.
DR SMR; Q7WY78; -.
DR STRING; 224308.BSU35840; -.
DR PaxDb; Q7WY78; -.
DR PRIDE; Q7WY78; -.
DR DNASU; 936823; -.
DR EnsemblBacteria; CAB15601; CAB15601; BSU_35840.
DR GeneID; 936823; -.
DR KEGG; bsu:BSU35840; -.
DR PATRIC; fig|224308.179.peg.3880; -.
DR eggNOG; COG1316; Bacteria.
DR InParanoid; Q7WY78; -.
DR OMA; FTHAHAY; -.
DR PhylomeDB; Q7WY78; -.
DR BioCyc; BSUB:BSU35840-MON; -.
DR BioCyc; MetaCyc:BSU35840-MON; -.
DR EvolutionaryTrace; Q7WY78; -.
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 InterPro; IPR004474; LytR_CpsA_psr.
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..322
FT /note="Polyisoprenyl-teichoic acid--peptidoglycan teichoic
FT acid transferase TagT"
FT /id="PRO_0000049997"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 20..40
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..322
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:6MPT"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:6MPT"
FT STRAND 96..105
FT /evidence="ECO:0007829|PDB:6MPT"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:6MPT"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:6MPT"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:6MPT"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:6MPT"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:6MPT"
FT HELIX 134..152
FT /evidence="ECO:0007829|PDB:6MPT"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:6MPT"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:6MPT"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:6MPT"
FT HELIX 184..193
FT /evidence="ECO:0007829|PDB:6MPT"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:6MPT"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:6MPT"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:6MPT"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:6MPT"
FT HELIX 225..242
FT /evidence="ECO:0007829|PDB:6MPT"
FT TURN 257..260
FT /evidence="ECO:0007829|PDB:6MPT"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:6MPT"
FT HELIX 268..278
FT /evidence="ECO:0007829|PDB:6MPT"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:6MPT"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:6MPT"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:6MPS"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:6MPT"
FT HELIX 306..319
FT /evidence="ECO:0007829|PDB:6MPT"
SQ SEQUENCE 322 AA; 35921 MW; 7FF1DA1764ABE608 CRC64;
MEERSQRRKK KRKLKKWVKV VAGLMAFLVI AAGSVGAYAF VKLNNASKEA HVSLARGEQS
VKRIKEFDPG KDSFSVLLLG IDAREKNGET VDQARSDANV LVTFNRKEKT AKMLSIPRDA
YVNIPGHGYD KFTHAHAYGG VDLTVKTVEE MLDIPVDYVV ESNFTAFEDV VNELNGVKVT
VKSDKVIQQI KKDTKGKVVL QKGTHTLDGE EALAYVRTRK ADSDLLRGQR QMEVLSAIID
KSKSLSSIPA YDDIVDTMGQ NLKMNLSLKD AIGLFPFITS LKSVESIQLT GYDYEPAGVY
YFKLNQQKLQ EVKKELQNDL GV
