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YGFX_ECOLI
ID   YGFX_ECOLI              Reviewed;         135 AA.
AC   Q46824; Q2M9U5;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Inner membrane protein YgfX;
DE   AltName: Full=Toxin CptA {ECO:0000303|PubMed:22239607};
GN   Name=ygfX {ECO:0000303|PubMed:22474332};
GN   Synonyms=cptA {ECO:0000303|PubMed:22239607};
GN   OrderedLocusNames=b2896, JW2864;
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=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   [2]
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   [3]
RP   PRELIMINARY (INCORRECT) FUNCTION AS A TOXIN, SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH FTSZ AND MREB.
RC   STRAIN=B / BL21-DE3, and K12 / BW25113;
RX   PubMed=22239607; DOI=10.1111/j.1574-6968.2012.02496.x;
RA   Masuda H., Tan Q., Awano N., Yamaguchi Y., Inouye M.;
RT   "A novel membrane-bound toxin for cell division, CptA (YgfX), inhibits
RT   polymerization of cytoskeleton proteins, FtsZ and MreB, in Escherichia
RT   coli.";
RL   FEMS Microbiol. Lett. 328:174-181(2012).
RN   [4]
RP   FUNCTION.
RC   STRAIN=K12 / BW25113;
RX   PubMed=22474332; DOI=10.1074/jbc.m111.293803;
RA   McNeil M.B., Clulow J.S., Wilf N.M., Salmond G.P., Fineran P.C.;
RT   "SdhE is a conserved protein required for flavinylation of succinate
RT   dehydrogenase in bacteria.";
RL   J. Biol. Chem. 287:18418-18428(2012).
RN   [5]
RP   NOT A TOXIN-ANTITOXIN SYSTEM, AND FUNCTION.
RC   STRAIN=K12 / BW25113;
RX   PubMed=23657679; DOI=10.1099/mic.0.068510-0;
RA   McNeil M.B., Iglesias-Cans M.C., Clulow J.S., Fineran P.C.;
RT   "YgfX (CptA) is a multimeric membrane protein that interacts with the
RT   succinate dehydrogenase assembly factor SdhE (YgfY).";
RL   Microbiology 159:1352-1365(2013).
CC   -!- FUNCTION: A probable inner membrane protein. Has been shown not to be a
CC       toxin, no effects on growth are seen in LB or minimal medium up to 6 or
CC       21 hours (respectively) after induction of expression
CC       (PubMed:23657679). Interacts with cytoskeletal proteins FtsZ and MreB;
CC       inhibits FtsZ GTP-dependent polymerization as well as MreB ATP-
CC       dependent polymerization (PubMed:22239607). Restores production of
CC       prodigiosin antibiotic (Pig) in Serratia strains with deletions of
CC       sdhE-ygfX; overexpression of this protein and CptB also restores Pig
CC       production to a slightly lesser extent in Serratia (PubMed:22474332).
CC       {ECO:0000269|PubMed:22239607, ECO:0000269|PubMed:22474332,
CC       ECO:0000269|PubMed:23657679}.
CC   -!- SUBUNIT: Interacts with MreB and FtsZ; interaction with the latter
CC       requires FtsZ residues 33-49 (PubMed:22239607).
CC       {ECO:0000269|PubMed:22239607}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:22239607}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:22239607}.
CC   -!- CAUTION: Was originally thought to be the toxic component of a type II
CC       toxin-antitoxin (TA) system; overexpression was shown to lead to growth
CC       arrest after 5 hours, with initial elongation of cells, followed by
CC       swelling (PubMed:22239607). The toxic effects were abrogated by
CC       coexpression with antitoxin CptB (now sdhE) (PubMed:22239607). However
CC       subsequent studies have been unable to show the toxic effect upon
CC       overexpression, nor is the Serratia ortholog a toxin (PubMed:23657679).
CC       {ECO:0000269|PubMed:22239607, ECO:0000269|PubMed:23657679}.
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DR   EMBL; U28375; AAA83077.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75934.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76961.1; -; Genomic_DNA.
DR   PIR; H65073; H65073.
DR   RefSeq; NP_417372.1; NC_000913.3.
DR   RefSeq; WP_000244777.1; NZ_STEB01000001.1.
DR   AlphaFoldDB; Q46824; -.
DR   BioGRID; 4262341; 9.
DR   IntAct; Q46824; 1.
DR   STRING; 511145.b2896; -.
DR   jPOST; Q46824; -.
DR   PaxDb; Q46824; -.
DR   PRIDE; Q46824; -.
DR   EnsemblBacteria; AAC75934; AAC75934; b2896.
DR   EnsemblBacteria; BAE76961; BAE76961; BAE76961.
DR   GeneID; 947379; -.
DR   KEGG; ecj:JW2864; -.
DR   KEGG; eco:b2896; -.
DR   PATRIC; fig|1411691.4.peg.3837; -.
DR   EchoBASE; EB2884; -.
DR   eggNOG; ENOG502ZSY3; Bacteria.
DR   HOGENOM; CLU_153203_0_0_6; -.
DR   OMA; WLASDSM; -.
DR   PhylomeDB; Q46824; -.
DR   BioCyc; EcoCyc:G7509-MON; -.
DR   PRO; PR:Q46824; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR   GO; GO:0032091; P:negative regulation of protein binding; IDA:EcoCyc.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   InterPro; IPR009883; YgfX.
DR   Pfam; PF07254; Cpta_toxin; 1.
DR   PIRSF; PIRSF020653; UCP020653; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Cell shape; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..135
FT                   /note="Inner membrane protein YgfX"
FT                   /id="PRO_0000169359"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..37
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        55..135
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..96
FT                   /note="Not required to inhibit FtsZ or MreB polymerization"
SQ   SEQUENCE   135 AA;  16064 MW;  CB3D38F10AAD1D98 CRC64;
     MVLWQSDLRV SWRAQWLSLL IHGLVAAVIL LMPWPLSYTP LWMVLLSLVV FDCVRSQRRI
     NARQGEIRLL MDGRLRWQGQ EWSIVKAPWM IKSGMMLRLR SDGGKRQHLW LAADSMDEAE
     WRDLRRILLQ QETQR
 
 
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