IF2_PSEPG
ID IF2_PSEPG Reviewed; 842 AA.
AC B0KHX8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=PputGB1_4712;
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-2008) 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; CP000926; ABZ00599.1; -; Genomic_DNA.
DR RefSeq; WP_012274244.1; NC_010322.1.
DR AlphaFoldDB; B0KHX8; -.
DR SMR; B0KHX8; -.
DR STRING; 76869.PputGB1_4712; -.
DR EnsemblBacteria; ABZ00599; ABZ00599; PputGB1_4712.
DR KEGG; ppg:PputGB1_4712; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_1_6; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000002157; 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; 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..842
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000075614"
FT DOMAIN 342..509
FT /note="tr-type G"
FT REGION 94..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..358
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 376..380
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 397..400
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 451..454
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 487..489
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 173..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 351..358
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 397..401
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 451..454
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 842 AA; 91179 MW; 22906692EB02EE55 CRC64;
MTQVTVKELA QEVEAPVERL LQQMREAGLP HTDAGQVVTD NEKQTLLTHL KSSHKSKAEE
PRKITLQRKT TSTLRVAGSK SISVEVRKKK VFVQRSPEEI QAEQKRELDE RRAAENAARD
KVEAEVRQRN EEQARRQAAD SAVAAPAPAA KPEPAPAAAP APVVADAPAS EDAAARAAER
KKDETRRNES RTRDDDRRRG EAPRVSIKVK VKEKEKAPTP RAAPRTTDEE SDGARRGRGG
KGKLKKRNQH GFQNPTGPVI RDVTIGETIT VSELANQMSV KGAEVVKFMF KMGTPVTINQ
VLDQETAQLI AEELGHKVTL VSDTALEDSL AESLKFEGQT ESRAPVVTVM GHVDHGKTSL
LDYIRRAKVA AGEAGGITQH IGAYHVETDR GMVTFLDTPG HAAFTQMRAR GAKATDIVIL
VVAADDGVMP QTREAVQHAK AAGVPLVVAV NKIDKPGADL DRIRNELSVE GVTSEDWGGD
TPFVKVSAKM GTGVDELLEA VLLQAEILEL TATPTAPGRG VVVESRLDKG RGPVATILVQ
DGTLRQGDMV LCGSNYGRVR AMLDENGKPV KEAGPSIPVE ILGLDGTPEA GDELSVVADE
KKAREVALFR QGKYREVKLA RAHAGKLENI FETMGQEEKK TLNIVLKTDV RGSLEALQGS
LGGLGNDEVQ VRVIGGGVGG ITESDANLAL ASNAVLFGFN VRADAGARKI VEQEGLDMRY
YNVIYDIIED VKKALTGMLG SDVRENILGV AEVRDVFRSP KFGAIAGCMV IEGTVYRNRP
IRVLRDDVVI FEGELESLRR FKDDASEVRS GMECGIGVKS YNDVKVGDKI EVFEKVQVAR
TL
