IF2_PSEP1
ID IF2_PSEP1 Reviewed; 846 AA.
AC A5W987;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Pput_4577;
OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-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; CP000712; ABQ80697.1; -; Genomic_DNA.
DR RefSeq; WP_004575779.1; NC_009512.1.
DR AlphaFoldDB; A5W987; -.
DR SMR; A5W987; -.
DR STRING; 351746.Pput_4577; -.
DR PRIDE; A5W987; -.
DR EnsemblBacteria; ABQ80697; ABQ80697; Pput_4577.
DR KEGG; ppf:Pput_4577; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_1_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
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; 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 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..846
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008306"
FT DOMAIN 346..513
FT /note="tr-type G"
FT REGION 94..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..362
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 380..384
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 401..404
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 455..458
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 491..493
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 94..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 355..362
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 401..405
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 455..458
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 846 AA; 91505 MW; 3E0A4FDC23738C10 CRC64;
MTQVTVKELA QEVEAPVERL LQQMREAGLP HTDAGQVVTD NEKQTLLTHL KSSHKSKAEE
PRKITLQRKT TSTLRVAGSK SISVEVRKKK VFVQRSPEEI QAEQKRELEE RRAAENAARD
KVEAEVRQRN EEQARRQAAG STAAAPAPAA KPEPAPAAAP VAAPAPVVAD APASEDAAAR
AAERKKDETR RNESRTRDDD RRRGEAPRVS IKVKVKEKEK APTPRAAPRT TDEESDGARR
GRGGKSKLKK RNQHGFQNPT GPVIRDVTIG ETITVSELAN QMSVKGAEVV KFMFKMGTPV
TINQVLDQET AQLIAEELGH KVTLVSDTAL EDSLAESLKF EGQTESRAPV VTVMGHVDHG
KTSLLDYIRR AKVAAGEAGG ITQHIGAYHV ETDRGMVTFL DTPGHAAFTQ MRARGAKATD
IVILVVAADD GVMPQTREAV QHAKAAGVPL VVAVNKIDKP GADLDRIRNE LSVEGVTSED
WGGDTPFVKV SAKMGTGVDE LLEAVLLQAE ILELTATPTA PGRGVVVESR LDKGRGPVAT
ILVQDGTLRQ GDMVLCGSNY GRVRAMLDEN GKPVKEAGPS IPVEILGLDG TPEAGDELSV
VADEKKAREV ALFRQGKYRE VKLARAHAGK LENIFETMGQ EEKKTLNIVL KTDVRGSLEA
LQGSLGGLGN DEVQVRVIGG GVGGITESDA NLALASNAVL FGFNVRADAG ARKIVEQEGL
DMRYYNVIYD IIEDVKKALT GMLGSDVREN ILGVAEVRDV FRSPKFGAIA GCMVIEGTVY
RNRPIRVLRD DVVIFEGELE SLRRFKDDAS EVRSGMECGI GVKSYNDVKV GDKIEVFEKV
QVARTL
