IF2_PSEPF
ID IF2_PSEPF Reviewed; 837 AA.
AC Q3KI84;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Pfl01_0779;
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=205922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf0-1;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
CC -!- FUNCTION: One of the essential components for the initiation of protein
CC synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC and promotes its binding to the 30S ribosomal subunits. Also involved
CC in the hydrolysis of GTP during the formation of the 70S ribosomal
CC complex. {ECO:0000255|HAMAP-Rule:MF_00100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00100}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00100}.
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DR EMBL; CP000094; ABA72522.1; -; Genomic_DNA.
DR RefSeq; WP_011332408.1; NC_007492.2.
DR AlphaFoldDB; Q3KI84; -.
DR SMR; Q3KI84; -.
DR STRING; 205922.Pfl01_0779; -.
DR PRIDE; Q3KI84; -.
DR EnsemblBacteria; ABA72522; ABA72522; Pfl01_0779.
DR KEGG; pfo:Pfl01_0779; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000002704; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
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; 1.
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 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..837
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228230"
FT DOMAIN 337..506
FT /note="tr-type G"
FT REGION 94..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..353
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 371..375
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 392..395
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 446..449
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 482..484
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 94..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 346..353
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 392..396
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 446..449
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 837 AA; 90304 MW; F1791F0125C33175 CRC64;
MTQVTVKQLA DEVKTPVERL LQQMREAGLP HTAAEENVTD SEKQSLLTHL KSSHKAKVEE
PRKITLQRKT TSTLRVAGSK SISVEVRKKK VFVQRSPEEI EAERKRELDE RRAVENAARQ
KAEEEARVRA EEEARRQPAA PSAPAEAVAA PAPVAEPVRE AAPVVAAAPA ADTRKRDEQR
RPDKPRADDN NRRGGDGERK NAPHRASVKE KAPAPRVAPR TTDEESDGFR RGGRGKAKLK
KRNAHGFQSP TGPVVREVKI GETITVGDLA QQMSVKAAEI IKFMFKLGTP ATINQVLDQE
TAQLVAEELG HKVTLVSDTA LEDSLAESLK FEGEAVPRAP VVTVMGHVDH GKTSLLDYIR
RAKVAAGEAG GITQHIGAYH VETERGMVTF LDTPGHAAFT AMRARGAKAT DIVILVVAAD
DGVMPQTIEA VQHAVAAGVP LVVAVNKIDK PGADLDRIRS ELSAHGVTSE DWGGDTPFVP
VSAKMGTGVD ELLEAVLLQA EVLELTATPS APGRGVVVES RLDKGRGPVA TVLVQDGTLR
QGDMVLVGSN YGRVRAMLDE NGKPIKEAGP AIPVEILGLD GTPDAGDEMS VVADEKKARE
VALFRQGKFR EVKLARAHAG KLENIFESMG QEEKKTLNIV LKSDVRGSLE ALQGALNGLG
NDEVQVRVVG GGVGGITESD ANLALASNAV LFGFNVRADA GARKIVEQEG LDMRYYNVIY
DIIEDVKKAL TGMLGSDVRE NILGVAEVRD VFRSPKFGAI AGCMVIEGTV HRNRPIRVLR
EDIVIFEGEL ESLRRFKDDA SEVRAGMECG IGVKSYNDVK VGDKIEVFEK VQVARSL
