IF2_PSEA7
ID IF2_PSEA7 Reviewed; 837 AA.
AC A6VCK1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=PSPA7_5462;
OS Pseudomonas aeruginosa (strain PA7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=381754;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA7;
RA Dodson R.J., Harkins D., Paulsen I.T.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000744; ABR85823.1; -; Genomic_DNA.
DR RefSeq; WP_003148734.1; NC_009656.1.
DR AlphaFoldDB; A6VCK1; -.
DR SMR; A6VCK1; -.
DR EnsemblBacteria; ABR85823; ABR85823; PSPA7_5462.
DR KEGG; pap:PSPA7_5462; -.
DR HOGENOM; CLU_006301_6_1_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001582; 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_1000008302"
FT DOMAIN 337..506
FT /note="tr-type G"
FT REGION 94..253
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..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..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; 90643 MW; 2ED4A2B9423C060E CRC64;
MTQVTVKELA QVVDTPVERL LLQMRDAGLP HTSAEQVVTD SEKQALLTHL KGSHGDRASE
PRKITLQRKT TTTLKVGGSK TVSVEVRKKK TYVKRSPDEI EAERQRELEE QRAAEEAERL
KAEEAAARQR AEEEARKAEE AARAKAAEEA VSAQPAAAVE VAAAEPVAKP AAAEERKKEE
PRRVPKRDED DERRDRKHTQ HRPSVKEKEK APAPRVAPRS TDEESDGYRR GGRGGKSKLK
KRNQHGFQNP TGPIVREVNI GETITVAELA AQMSVKGAEV VKFMFKMGSP VTINQVLDQE
TAQLVAEELG HKVKLVSENA LEEQLAESLK FEGEAVTRAP VVTVMGHVDH GKTSLLDYIR
RAKVAAGEAG GITQHIGAYH VETERGMVTF LDTPGHAAFT AMRARGAQAT DIVILVVAAD
DGVMPQTQEA VQHAKAAGVP IVVAVNKIDK PEANPDNIKN GLAALDVIPE EWGGDAPFVP
VSAKLGTGVD ELLEAVLLQA EVLELKATPS APGRGVVVES RLDKGRGPVA TVLVQDGTLR
QGDMVLVGIN YGRVRAMLDE NGKPIKEAGP SIPVEILGLD GTPDAGDEMT VVADEKKARE
VALFRQGKFR EVKLARAHAG KLENIFENMG QEEKKTLNIV LKADVRGSLE ALQGSLSGLG
NDEVQVRVVG GGVGGITESD ANLALASNAV LFGFNVRADA GARKIVEAEG LDMRYYNVIY
DIIEDVKKAL TGMLGSDLRE NILGIAEVRD VFRSPKFGAI AGCMVTEGMV HRNRPIRVLR
DDVVIFEGEL ESLRRFKDDV AEVRAGMECG IGVKSYNDVK VGDKIEVFEK VEVARSL
