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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
 
 
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