IF2_ECOLI
ID IF2_ECOLI Reviewed; 890 AA.
AC P0A705; O32548; O32549; O32550; O34379; O34415; O34603; P02995; Q2M942;
AC Q9EUZ4; Q9EUZ5; Q9EUZ6; Q9EUZ8; Q9EUZ9; Q9EV00;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB; Synonyms=gicD, ssyG; OrderedLocusNames=b3168, JW3137;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6096856; DOI=10.1073/pnas.81.24.7787;
RA Sacerdot C., Dessen P., Hershey J.W.B., Plumbridge J.A.,
RA Grunberg-Manago M.;
RT "Sequence of the initiation factor IF2 gene: unusual protein features and
RT homologies with elongation factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:7787-7791(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Various clinical strains;
RX PubMed=9428651; DOI=10.1016/s0014-5793(97)01472-5;
RA Steffensen S.A.D.A., Poulsen A.B., Mortensen K.K., Sperling-Petersen H.U.;
RT "E. coli translation initiation factor IF2--an extremely conserved protein.
RT Comparative sequence analysis of the infB gene in clinical isolates of E.
RT coli.";
RL FEBS Lett. 419:281-284(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IQ489, and IQ490;
RA Hedegaard J., Kristensen J.E., Nakamura Y., Sperling-Petersen H.U.,
RA Mortensen K.K.;
RT "Sequence of the infB gene from Escherichia coli strain IQ489 and IQ490.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RX PubMed=6326058; DOI=10.1093/nar/12.7.3333;
RA Ishii S., Ihara M., Maekawa T., Nakamura Y., Uchida H., Imamoto F.;
RT "The nucleotide sequence of the cloned nusA gene and its flanking region of
RT Escherichia coli.";
RL Nucleic Acids Res. 12:3333-3342(1984).
RN [7]
RP PROTEIN SEQUENCE OF 1-11 AND 159-174 (ISOFORMS ALPHA AND BETA).
RX PubMed=3894004; DOI=10.1002/j.1460-2075.1985.tb02339.x;
RA Plumbridge J.A., Deville F., Sacerdot C., Petersen H.U., Cenatiempo Y.,
RA Cozzone A., Grunberg-Manago M., Hershey J.W.;
RT "Two translational initiation sites in the infB gene are used to express
RT initiation factor IF2 alpha and IF2 beta in Escherichia coli.";
RL EMBO J. 4:223-229(1985).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 864-890, INDUCTION, AND OPERON.
RC STRAIN=K12;
RX PubMed=2849753; DOI=10.1093/nar/16.22.10803;
RA Sands J.F., Regnier P., Cummings H.S., Grunberg-Manago M., Hershey J.W.B.;
RT "The existence of two genes between infB and rpsO in the Escherichia coli
RT genome: DNA sequencing and S1 nuclease mapping.";
RL Nucleic Acids Res. 16:10803-10816(1988).
RN [9]
RP PROTEIN SEQUENCE OF 159-174 AND 166-174 (ISOFORMS BETA AND BETA'),
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1764105; DOI=10.1016/0006-291x(91)92118-4;
RA Nyengaard N.R., Mortensen K.K., Lassen S.F., Hershey J.W.B.,
RA Sperling-Petersen H.U.;
RT "Tandem translation of E. coli initiation factor IF2 beta: purification and
RT characterization in vitro of two active forms.";
RL Biochem. Biophys. Res. Commun. 181:1572-1579(1991).
RN [10]
RP PROTEIN SEQUENCE OF 159-169 AND 166-171 (ISOFORMS BETA AND BETA'),
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF VAL-158 AND MET-165.
RX PubMed=1374802; DOI=10.1016/0022-2836(92)91026-l;
RA Sacerdot C., Vachon G., Laalami S., Morel-Deville F., Cenatiempo Y.,
RA Grunberg-Manago M.;
RT "Both forms of translational initiation factor IF2 (alpha and beta) are
RT required for maximal growth of Escherichia coli. Evidence for two
RT translational initiation codons for IF2 beta.";
RL J. Mol. Biol. 225:67-80(1992).
RN [11]
RP PROTEIN SEQUENCE OF 290-304, FUNCTION, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=2444251; DOI=10.1021/bi00390a028;
RA Cenatiempo Y., Deville F., Dondon J., Grunberg-Manago M., Sacerdot C.,
RA Hershey J.W., Hansen H.F., Petersen H.U., Clark B.F., Kjeldgaard M.;
RT "The protein synthesis initiation factor 2 G-domain. Study of a
RT functionally active C-terminal 65-kilodalton fragment of IF2 from
RT Escherichia coli.";
RL Biochemistry 26:5070-5076(1987).
RN [12]
RP DOMAIN STRUCTURE, AND REVIEW.
RX PubMed=1805969; DOI=10.1016/0300-9084(91)90191-3;
RA Laalami S., Sacerdot C., Vachon G., Mortensen K., Sperling-Petersen H.U.,
RA Cenatiempo Y., Grunberg-Manago M.;
RT "Structural and functional domains of E coli initiation factor IF2.";
RL Biochimie 73:1557-1566(1991).
RN [13]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [14]
RP PARTIALLY SUPPRESSES A RSGA MUTANT.
RC STRAIN=K12;
RX PubMed=18223068; DOI=10.1128/jb.01744-07;
RA Campbell T.L., Brown E.D.;
RT "Genetic interaction screens with ordered overexpression and deletion clone
RT sets implicate the Escherichia coli GTPase YjeQ in late ribosome
RT biogenesis.";
RL J. Bacteriol. 190:2537-2545(2008).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-808, 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).
RN [16]
RP FUNCTION, AND SUBUNIT.
RX PubMed=20224578; DOI=10.1038/embor.2010.12;
RA Milon P., Carotti M., Konevega A.L., Wintermeyer W., Rodnina M.V.,
RA Gualerzi C.O.;
RT "The ribosome-bound initiation factor 2 recruits initiator tRNA to the 30S
RT initiation complex.";
RL EMBO Rep. 11:312-316(2010).
RN [17]
RP FUNCTION, AND SUBUNIT.
RX PubMed=22562136; DOI=10.1038/nsmb.2285;
RA Milon P., Maracci C., Filonava L., Gualerzi C.O., Rodnina M.V.;
RT "Real-time assembly landscape of bacterial 30S translation initiation
RT complex.";
RL Nat. Struct. Mol. Biol. 19:609-615(2012).
RN [18]
RP REVIEW.
RX PubMed=22515367; DOI=10.3109/10409238.2012.678284;
RA Milon P., Rodnina M.V.;
RT "Kinetic control of translation initiation in bacteria.";
RL Crit. Rev. Biochem. Mol. Biol. 47:334-348(2012).
RN [19]
RP STRUCTURE BY NMR OF 2-50.
RC STRAIN=K12;
RX PubMed=12600987; DOI=10.1074/jbc.m212960200;
RA Laursen B.S., Mortensen K.K., Sperling-Petersen H.U., Hoffman D.W.;
RT "A conserved structural motif at the N terminus of bacterial translation
RT initiation factor IF2.";
RL J. Biol. Chem. 278:16320-16328(2003).
RN [20]
RP MODEL BY ELECTRON MICROSCOPY (18.3 ANGSTROMS), AND SUBUNIT.
RX PubMed=21750663; DOI=10.1371/journal.pbio.1001095;
RA Julian P., Milon P., Agirrezabala X., Lasso G., Gil D., Rodnina M.V.,
RA Valle M.;
RT "The cryo-EM structure of a complete 30S translation initiation complex
RT from Escherichia coli.";
RL PLoS Biol. 9:E1001095-E1001095(2011).
CC -!- FUNCTION: One of the essential components for the initiation of protein
CC synthesis. May protect N-formylmethionyl-tRNA(fMet) from spontaneous
CC hydrolysis. Promotes N-formylmethionyl-tRNA(fMet) binding to the 30S
CC pre-initiation complex (PIC) (PubMed:1764105, PubMed:20224578). Also
CC involved in the hydrolysis of GTP during the formation of the 70S
CC ribosomal complex. Upon addition of the 50S ribosomal subunit, IF-1,
CC IF-2 and IF-3 are released leaving the mature 70S translation
CC initiation complex. {ECO:0000269|PubMed:1764105,
CC ECO:0000269|PubMed:20224578, ECO:0000269|PubMed:22562136,
CC ECO:0000269|PubMed:2444251}.
CC -!- SUBUNIT: Component of the 30S ribosomal translation pre-initiation
CC complex which assembles on the 30S ribosome in the order IF-2 and IF-3,
CC IF-1 and N-formylmethionyl-tRNA(fMet); mRNA recruitment can occur at
CC any time during PIC assembly. {ECO:0000269|PubMed:20224578,
CC ECO:0000269|PubMed:21750663, ECO:0000269|PubMed:22562136}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1764105}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=3;
CC Name=Alpha {ECO:0000269|PubMed:3894004};
CC IsoId=P0A705-1; Sequence=Displayed;
CC Name=Beta {ECO:0000269|PubMed:1374802, ECO:0000269|PubMed:1764105,
CC ECO:0000269|PubMed:3894004};
CC IsoId=P0A705-2; Sequence=VSP_018758, VSP_018759;
CC Name=Beta' {ECO:0000269|PubMed:1374802, ECO:0000269|PubMed:1764105};
CC IsoId=P0A705-3; Sequence=VSP_018760;
CC -!- INDUCTION: Part of the metY operon that extends to pnp
CC (PubMed:2849753). {ECO:0000269|PubMed:2849753}.
CC -!- PTM: A proteolyzed form, called IF2 gamma (begins with residue 290),
CC can be detected during purification which has all the activities
CC expected for this protein, although it is slightly less efficient than
CC full-length protein. It is not clear if it exists in vivo.
CC {ECO:0000269|PubMed:2444251}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted. The C-terminal
CC region (residues 165-890) is sufficient for growth at 42 degrees
CC Celsius, although it grows more slowly at 37 degrees and is cold-
CC sensitive at 30 degrees Celsius (PubMed:1374802).
CC {ECO:0000269|PubMed:1374802}.
CC -!- MISCELLANEOUS: When overexpressed partially suppresses the slow growth
CC and decreased 70S ribosome phenotype of an rsgA knockout; RsgA may be
CC involved in 30S ribosomal subunit biogenesis.
CC {ECO:0000269|PubMed:18223068}.
CC -!- MISCELLANEOUS: Silent mutations of codon 158, which no longer function
CC as alternative start codons, decrease beta isoform expression to 31 to
CC 50%, the strongest mutation is GUG to GUC.
CC {ECO:0000269|PubMed:1374802}.
CC -!- MISCELLANEOUS: [Isoform Alpha]: Isoform alpha is approximately 2-fold
CC more abundant than the combined beta isoforms. Optimal growth requires
CC both alpha and beta IF2. {ECO:0000305|PubMed:1374802}.
CC -!- MISCELLANEOUS: [Isoform Beta]: Also called beta1.
CC {ECO:0000305|PubMed:1374802}.
CC -!- MISCELLANEOUS: [Isoform Beta']: Also called beta2.
CC {ECO:0000305|PubMed:1374802}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
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DR EMBL; X00513; CAA25201.1; -; Genomic_DNA.
DR EMBL; X00513; CAA25202.1; -; Genomic_DNA.
DR EMBL; U18997; AAA57971.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76202.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77214.1; -; Genomic_DNA.
DR EMBL; AJ002537; CAA05529.1; -; Genomic_DNA.
DR EMBL; AJ002537; CAA05530.1; -; Genomic_DNA.
DR EMBL; AJ002537; CAA05531.1; -; Genomic_DNA.
DR EMBL; AJ002538; CAA05532.1; -; Genomic_DNA.
DR EMBL; AJ002538; CAA05533.1; -; Genomic_DNA.
DR EMBL; AJ002538; CAA05534.1; -; Genomic_DNA.
DR EMBL; AJ002539; CAA05535.1; -; Genomic_DNA.
DR EMBL; AJ002539; CAA05536.1; -; Genomic_DNA.
DR EMBL; AJ002539; CAA05537.1; -; Genomic_DNA.
DR EMBL; AJ002540; CAA05538.1; -; Genomic_DNA.
DR EMBL; AJ002540; CAA05539.1; -; Genomic_DNA.
DR EMBL; AJ002540; CAA05540.1; -; Genomic_DNA.
DR EMBL; AJ002541; CAA05541.1; -; Genomic_DNA.
DR EMBL; AJ002541; CAA05542.1; -; Genomic_DNA.
DR EMBL; AJ002541; CAA05543.1; -; Genomic_DNA.
DR EMBL; AJ002542; CAA05544.1; -; Genomic_DNA.
DR EMBL; AJ002542; CAA05545.1; -; Genomic_DNA.
DR EMBL; AJ002542; CAA05546.1; -; Genomic_DNA.
DR EMBL; AJ002402; CAA05386.1; -; Genomic_DNA.
DR EMBL; AJ002403; CAA05387.1; -; Genomic_DNA.
DR EMBL; AJ002404; CAA05388.1; -; Genomic_DNA.
DR EMBL; AJ002405; CAA05389.1; -; Genomic_DNA.
DR EMBL; AJ002406; CAA05390.1; -; Genomic_DNA.
DR EMBL; AJ002407; CAA05391.1; -; Genomic_DNA.
DR EMBL; AJ002408; CAA05392.1; -; Genomic_DNA.
DR EMBL; AJ002409; CAA05393.1; -; Genomic_DNA.
DR EMBL; AJ002410; CAA05394.1; -; Genomic_DNA.
DR EMBL; AJ002411; CAA05395.1; -; Genomic_DNA.
DR EMBL; AJ002412; CAA05396.1; -; Genomic_DNA.
DR EMBL; AJ002413; CAA05397.1; -; Genomic_DNA.
DR EMBL; AJ132861; CAC20126.1; -; Genomic_DNA.
DR EMBL; AJ132861; CAC20127.1; -; Genomic_DNA.
DR EMBL; AJ132861; CAC20128.1; -; Genomic_DNA.
DR EMBL; AJ132862; CAC20130.1; -; Genomic_DNA.
DR EMBL; AJ132862; CAC20131.1; -; Genomic_DNA.
DR EMBL; AJ132862; CAC20132.1; -; Genomic_DNA.
DR EMBL; X13775; CAA32019.1; -; Genomic_DNA.
DR PIR; D65107; FIEC2.
DR RefSeq; NP_417637.1; NC_000913.3.
DR RefSeq; WP_000133044.1; NZ_STEB01000012.1.
DR PDB; 1ND9; NMR; -; A=2-50.
DR PDB; 1ZO1; EM; 13.80 A; I=388-888.
DR PDB; 3JCJ; EM; 3.70 A; f=1-890.
DR PDB; 3JCN; EM; 4.60 A; b=1-890.
DR PDB; 5ME0; EM; 13.50 A; W=1-890.
DR PDB; 5ME1; EM; 13.50 A; W=1-890.
DR PDB; 6O9K; EM; 4.00 A; z=382-890.
DR PDBsum; 1ND9; -.
DR PDBsum; 1ZO1; -.
DR PDBsum; 3JCJ; -.
DR PDBsum; 3JCN; -.
DR PDBsum; 5ME0; -.
DR PDBsum; 5ME1; -.
DR PDBsum; 6O9K; -.
DR AlphaFoldDB; P0A705; -.
DR SMR; P0A705; -.
DR BioGRID; 4262436; 45.
DR ComplexPortal; CPX-2244; Translation initiation factor complex.
DR DIP; DIP-36182N; -.
DR IntAct; P0A705; 52.
DR STRING; 511145.b3168; -.
DR iPTMnet; P0A705; -.
DR jPOST; P0A705; -.
DR PaxDb; P0A705; -.
DR PRIDE; P0A705; -.
DR EnsemblBacteria; AAC76202; AAC76202; b3168.
DR EnsemblBacteria; BAE77214; BAE77214; BAE77214.
DR GeneID; 58462836; -.
DR GeneID; 947684; -.
DR KEGG; ecj:JW3137; -.
DR KEGG; eco:b3168; -.
DR PATRIC; fig|511145.12.peg.3263; -.
DR EchoBASE; EB0500; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR InParanoid; P0A705; -.
DR OMA; NRDNRTG; -.
DR PhylomeDB; P0A705; -.
DR BioCyc; EcoCyc:EG10505-MON; -.
DR BRENDA; 3.6.5.3; 2026.
DR EvolutionaryTrace; P0A705; -.
DR PRO; PR:P0A705; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:EcoCyc.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR GO; GO:0043024; F:ribosomal small subunit binding; IDA:EcoCyc.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:EcoliWiki.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:EcoCyc.
DR GO; GO:0009409; P:response to cold; IDA:EcoCyc.
DR GO; GO:0006413; P:translational initiation; IDA:EcoCyc.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR006847; IF2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR000178; TF_IF2_bacterial-like.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF46955; SSF46955; 1.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00487; IF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation; Cytoplasm;
KW Direct protein sequencing; GTP-binding; Initiation factor;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..890
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000238785"
FT DOMAIN 389..558
FT /note="tr-type G"
FT REGION 1..103
FT /note="1"
FT REGION 45..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..287
FT /note="2"
FT REGION 288..391
FT /note="3"
FT REGION 398..405
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 423..427
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 444..447
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 498..501
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 534..536
FT /note="G5"
FT /evidence="ECO:0000250"
FT REGION 541..668
FT /note="5"
FT REGION 669..890
FT /note="6"
FT COMPBIAS 45..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 398..405
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 444..448
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 498..501
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 808
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT VAR_SEQ 1..164
FT /note="Missing (in isoform Beta')"
FT /evidence="ECO:0000269|PubMed:1374802,
FT ECO:0000269|PubMed:1764105, ECO:0000305"
FT /id="VSP_018760"
FT VAR_SEQ 1..157
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000269|PubMed:1374802,
FT ECO:0000269|PubMed:1764105, ECO:0000269|PubMed:3894004,
FT ECO:0000305"
FT /id="VSP_018758"
FT VAR_SEQ 158
FT /note="V -> M (in isoform Beta)"
FT /evidence="ECO:0000305|PubMed:1764105,
FT ECO:0000305|PubMed:3894004"
FT /id="VSP_018759"
FT VARIANT 409
FT /note="D -> E (in strain: IQ489)"
FT VARIANT 423
FT /note="G -> GG (in strain: IQ490)"
FT VARIANT 432
FT /note="H -> Q (in strain: ECOAU9326)"
FT VARIANT 490
FT /note="Q -> G (in strain: ECOAU9302, ECOAU9306, ECOAU9307
FT and ECOAU9309)"
FT VARIANT 684
FT /note="G -> A (in strain: ECOAU9306)"
FT MUTAGEN 158
FT /note="V->A: Produces 35% of isoform beta (i.e. only
FT beta2)."
FT /evidence="ECO:0000269|PubMed:1374802"
FT MUTAGEN 158
FT /note="V->E: Produces 70% of isoform beta (i.e. only
FT beta2)."
FT /evidence="ECO:0000269|PubMed:1374802"
FT MUTAGEN 158
FT /note="V->G: Produces 66% of isoform beta (i.e. only
FT beta2)."
FT /evidence="ECO:0000269|PubMed:1374802"
FT MUTAGEN 165
FT /note="M->I,T: Produces reduces amount of isoform beta
FT (i.e. only beta1). Reduced growth at 37 degrees Celsius,
FT greatly reduced growth at 30 degrees Celsius. Growth is
FT more impaired; when associated with silent V-158 GUG to
FT GUC."
FT /evidence="ECO:0000269|PubMed:1374802"
FT HELIX 8..13
FT /evidence="ECO:0007829|PDB:1ND9"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1ND9"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:1ND9"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:1ND9"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1ND9"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:1ND9"
SQ SEQUENCE 890 AA; 97350 MW; 86B9F9B2AE773DDE CRC64;
MTDVTIKTLA AERQTSVERL VQQFADAGIR KSADDSVSAQ EKQTLIDHLN QKNSGPDKLT
LQRKTRSTLN IPGTGGKSKS VQIEVRKKRT FVKRDPQEAE RLAAEEQAQR EAEEQARREA
EESAKREAQQ KAEREAAEQA KREAAEQAKR EAAEKDKVSN QQDDMTKNAQ AEKARREQEA
AELKRKAEEE ARRKLEEEAR RVAEEARRMA EENKWTDNAE PTEDSSDYHV TTSQHARQAE
DESDREVEGG RGRGRNAKAA RPKKGNKHAE SKADREEARA AVRGGKGGKR KGSSLQQGFQ
KPAQAVNRDV VIGETITVGE LANKMAVKGS QVIKAMMKLG AMATINQVID QETAQLVAEE
MGHKVILRRE NELEEAVMSD RDTGAAAEPR APVVTIMGHV DHGKTSLLDY IRSTKVASGE
AGGITQHIGA YHVETENGMI TFLDTPGHAA FTSMRARGAQ ATDIVVLVVA ADDGVMPQTI
EAIQHAKAAQ VPVVVAVNKI DKPEADPDRV KNELSQYGIL PEEWGGESQF VHVSAKAGTG
IDELLDAILL QAEVLELKAV RKGMASGAVI ESFLDKGRGP VATVLVREGT LHKGDIVLCG
FEYGRVRAMR NELGQEVLEA GPSIPVEILG LSGVPAAGDE VTVVRDEKKA REVALYRQGK
FREVKLARQQ KSKLENMFAN MTEGEVHEVN IVLKADVQGS VEAISDSLLK LSTDEVKVKI
IGSGVGGITE TDATLAAASN AILVGFNVRA DASARKVIEA ESLDLRYYSV IYNLIDEVKA
AMSGMLSPEL KQQIIGLAEV RDVFKSPKFG AIAGCMVTEG VVKRHNPIRV LRDNVVIYEG
ELESLRRFKD DVNEVRNGME CGIGVKNYND VRTGDVIEVF EIIEIQRTIA
