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TABA_ECOLI
ID   TABA_ECOLI              Reviewed;         150 AA.
AC   P0AF96; P39335; Q2M657;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Toxin-antitoxin biofilm protein TabA;
GN   Name=tabA; Synonyms=yjgK; OrderedLocusNames=b4252, JW5756;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT   from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=B / BL21;
RX   PubMed=10493123;
RX   DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA   Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT   "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT   chromatography.";
RL   Electrophoresis 20:2181-2195(1999).
RN   [5]
RP   FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND GENE NAME.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=19060153; DOI=10.1128/jb.01465-08;
RA   Kim Y., Wang X., Ma Q., Zhang X.S., Wood T.K.;
RT   "Toxin-antitoxin systems in Escherichia coli influence biofilm formation
RT   through YjgK (TabA) and fimbriae.";
RL   J. Bacteriol. 191:1258-1267(2009).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX   PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA   Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA   Grishin N.V., Zhao Y.;
RT   "Lysine acetylation is a highly abundant and evolutionarily conserved
RT   modification in Escherichia coli.";
RL   Mol. Cell. Proteomics 8:215-225(2009).
CC   -!- FUNCTION: Influences biofilm formation. Represses fimbria genes in 8
CC       hours biofilms. May act in response to the combined activity of several
CC       toxin-antitoxin (TA) systems. {ECO:0000269|PubMed:19060153}.
CC   -!- INDUCTION: Induced by simultaneous deletion of five TA systems
CC       (MazF/MazE, RelE/RelB, ChpB, YoeB/YefM, and YafQ/DinJ).
CC       {ECO:0000269|PubMed:19060153}.
CC   -!- DISRUPTION PHENOTYPE: Deletion increases biofilm formation after 8
CC       hours and decreases biofilm formation after 24 hours.
CC       {ECO:0000269|PubMed:19060153}.
CC   -!- SIMILARITY: Belongs to the TabA/YiaL family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA97148.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U14003; AAA97148.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC77209.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78249.1; -; Genomic_DNA.
DR   PIR; S56477; S56477.
DR   RefSeq; NP_418673.4; NC_000913.3.
DR   RefSeq; WP_000583469.1; NZ_LN832404.1.
DR   AlphaFoldDB; P0AF96; -.
DR   SMR; P0AF96; -.
DR   BioGRID; 4259562; 211.
DR   DIP; DIP-48214N; -.
DR   STRING; 511145.b4252; -.
DR   iPTMnet; P0AF96; -.
DR   jPOST; P0AF96; -.
DR   PaxDb; P0AF96; -.
DR   PRIDE; P0AF96; -.
DR   EnsemblBacteria; AAC77209; AAC77209; b4252.
DR   EnsemblBacteria; BAE78249; BAE78249; BAE78249.
DR   GeneID; 58390508; -.
DR   GeneID; 948777; -.
DR   KEGG; ecj:JW5756; -.
DR   KEGG; eco:b4252; -.
DR   PATRIC; fig|1411691.4.peg.2452; -.
DR   EchoBASE; EB2420; -.
DR   eggNOG; COG2731; Bacteria.
DR   HOGENOM; CLU_107139_3_0_6; -.
DR   InParanoid; P0AF96; -.
DR   OMA; CLIKVLM; -.
DR   PhylomeDB; P0AF96; -.
DR   BioCyc; EcoCyc:G7883-MON; -.
DR   PRO; PR:P0AF96; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0044010; P:single-species biofilm formation; IMP:EcoCyc.
DR   Gene3D; 2.60.120.370; -; 1.
DR   InterPro; IPR004375; NanQ/TabA/YiaL.
DR   InterPro; IPR037012; NanQ/TabA/YiaL_sf.
DR   PANTHER; PTHR34986; PTHR34986; 1.
DR   Pfam; PF04074; DUF386; 1.
DR   TIGRFAMs; TIGR00022; TIGR00022; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Reference proteome.
FT   CHAIN           1..150
FT                   /note="Toxin-antitoxin biofilm protein TabA"
FT                   /id="PRO_0000169765"
FT   MOD_RES         36
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:18723842"
SQ   SEQUENCE   150 AA;  16865 MW;  30E316B24C523DAE CRC64;
     MIIGNIHNLQ PWLPQELRQA IEHIKAHVTA ETPKGKHDIE GNRLFYLISE DMTEPYEARR
     AEYHARYLDI QIVLKGQEGM TFSTQPAGAP DTDWLADKDI AFLPEGVDEK TVILNEGDFV
     VFYPGEVHKP LCAVGAPAQV RKAVVKMLMA
 
 
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