TAGV_BACSU
ID TAGV_BACSU Reviewed; 391 AA.
AC P96499; Q795D1;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Polyisoprenyl-teichoic acid--peptidoglycan teichoic acid transferase TagV {ECO:0000305};
DE EC=2.7.8.- {ECO:0000269|PubMed:21964069};
GN Name=tagV {ECO:0000303|PubMed:21964069}; Synonyms=yvhJ;
GN OrderedLocusNames=BSU35520;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Soldo B., Lazarevic V., Mauel C., Karamata D.;
RT "Sequence of the Bacillus subtilis 168 chromosomal region from 305 to 307
RT degree.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, PATHWAY, 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 [4] {ECO:0007744|PDB:3NXH}
RP X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS) OF 72-332.
RA Vorobiev S., Chen Y., Seetharaman J., Sahdev S., Xiao R., Ciccosanti C.,
RA Lee D., Everett J.K., Nair R., Acton T.B., Rost B., Montelione G.T.,
RA Hunt J.F., Tong L.;
RT "Crystal structure of the transcriptional regulator YvhJ from Bacillus
RT subtilis.";
RL Submitted (JUL-2010) to the PDB data bank.
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 -!- 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; U56901; AAC44935.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15569.1; -; Genomic_DNA.
DR PIR; H70041; H70041.
DR RefSeq; NP_391432.1; NC_000964.3.
DR RefSeq; WP_003244117.1; NZ_JNCM01000033.1.
DR PDB; 3NXH; X-ray; 2.58 A; A=72-332.
DR PDB; 6UF3; X-ray; 1.60 A; A=72-332.
DR PDBsum; 3NXH; -.
DR PDBsum; 6UF3; -.
DR AlphaFoldDB; P96499; -.
DR SMR; P96499; -.
DR STRING; 224308.BSU35520; -.
DR PaxDb; P96499; -.
DR PRIDE; P96499; -.
DR DNASU; 936761; -.
DR EnsemblBacteria; CAB15569; CAB15569; BSU_35520.
DR GeneID; 936761; -.
DR KEGG; bsu:BSU35520; -.
DR PATRIC; fig|224308.179.peg.3843; -.
DR eggNOG; COG1316; Bacteria.
DR InParanoid; P96499; -.
DR OMA; WRHNSNG; -.
DR PhylomeDB; P96499; -.
DR BioCyc; BSUB:BSU35520-MON; -.
DR BioCyc; MetaCyc:BSU35520-MON; -.
DR EvolutionaryTrace; P96499; -.
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..391
FT /note="Polyisoprenyl-teichoic acid--peptidoglycan teichoic
FT acid transferase TagV"
FT /id="PRO_0000391010"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 24..44
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..391
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 329..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 77..85
FT /evidence="ECO:0007829|PDB:6UF3"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:6UF3"
FT STRAND 96..105
FT /evidence="ECO:0007829|PDB:6UF3"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:6UF3"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:6UF3"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:6UF3"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:6UF3"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:6UF3"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:6UF3"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:6UF3"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:6UF3"
FT HELIX 167..176
FT /evidence="ECO:0007829|PDB:6UF3"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:6UF3"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:6UF3"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:6UF3"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:6UF3"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:6UF3"
FT HELIX 229..248
FT /evidence="ECO:0007829|PDB:6UF3"
FT HELIX 252..262
FT /evidence="ECO:0007829|PDB:6UF3"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:6UF3"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:6UF3"
FT HELIX 272..281
FT /evidence="ECO:0007829|PDB:6UF3"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:6UF3"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:6UF3"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:6UF3"
FT STRAND 297..302
FT /evidence="ECO:0007829|PDB:6UF3"
FT TURN 303..306
FT /evidence="ECO:0007829|PDB:6UF3"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:6UF3"
FT HELIX 314..328
FT /evidence="ECO:0007829|PDB:6UF3"
SQ SEQUENCE 391 AA; 43211 MW; DEF52D5308C54AD0 CRC64;
MAERVRVRVR KKKKSKRRKI LKRIMLLFAL ALLVVVGLGG YKLYKTINAA DESYDALSRG
NKSNLRNEVV DMKKKPFSIL FMGIEDYATK GQKGRSDSLI VVTLDPKNKT MKMLSIPRDT
RVQLAGDTTG SKTKINAAYS KGGKDETVET VENFLQIPID KYVTVDFDGF KDVINEVGGI
DVDVPFDFDE KSDVDESKRI YFKKGEMHLN GEEALAYARM RKQDKRGDFG RNDRQKQILN
ALIDRMSSAS NIAKIDKIAE KASENVETNI RITEGLALQQ IYSGFTSKKI DTLSITGSDL
YLGPNNTYYF EPDATNLEKV RKTLQEHLDY TPDTSTGTSG TEDGTDSSSS SGSTGSTGTT
TDGTTNGSSY SNDSSTSSNN STTNSTTDSS Y