IF2_PSEE4
ID IF2_PSEE4 Reviewed; 850 AA.
AC Q1IF43;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=PSEEN0795;
OS Pseudomonas entomophila (strain L48).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=384676;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L48;
RX PubMed=16699499; DOI=10.1038/nbt1212;
RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT "Complete genome sequence of the entomopathogenic and metabolically
RT versatile soil bacterium Pseudomonas entomophila.";
RL Nat. Biotechnol. 24:673-679(2006).
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; CT573326; CAK13711.1; -; Genomic_DNA.
DR RefSeq; WP_011532141.1; NC_008027.1.
DR AlphaFoldDB; Q1IF43; -.
DR SMR; Q1IF43; -.
DR STRING; 384676.PSEEN0795; -.
DR PRIDE; Q1IF43; -.
DR EnsemblBacteria; CAK13711; CAK13711; PSEEN0795.
DR KEGG; pen:PSEEN0795; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_1_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000658; 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..850
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008304"
FT DOMAIN 350..517
FT /note="tr-type G"
FT REGION 50..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..366
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 384..388
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 405..408
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 459..462
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 495..497
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 50..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 359..366
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 405..409
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 459..462
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 850 AA; 91915 MW; 124E4748055702C4 CRC64;
MTQVTVKELA QEVEAPVERL LQQMREAGLP HTDAGQVVTD NEKQTLLTHL KSSHKSKAEE
PRKITLQRKT TSTLRVAGSK SISVEVRKKK VFVQRSPEEI QAEQKREQEE RRAAENAARE
KADADARQRN EEQARRQAAQ APAAAPVAKA EPAPAAAAPA APAVPDAPVS EDAAARAAER
KKDEARRNES RTRDDDRRGG GVAGERRGEA PRVSIKVKVK EKEKAPTPRA APRTTDEESD
GFRRGRGGKG KPKKRNQHGF QNPTGPVIRD VTIGETITVS DLAQQMSVKG AEVVKFMFKL
GTPVTINQVL DQETAQLVAE ELGHKVTLVS DTALEDSLAE SLKFEGESES RAPVVTVMGH
VDHGKTSLLD YIRRAKVAAG EAGGITQHIG AYHVETDRGM VTFLDTPGHA AFTQMRARGA
KATDIVILVV AADDGVMPQT REAVQHAKAA GVPLVVAVNK IDKPGADLDR IRNELAVEGV
TSEDWGGDTP FVKVSAKMGT GVDELLEAVL LQAEILELKA TPTAPGRGVV VESRLDKGRG
PVATILVQDG TLRQGDMVLV GSNYGRVRAM LDENGKPVKE AGPSIPVEIL GLDGTPDAGD
EMSVVADEKK AREVALFRQG KYREVKLARA HAGKLENIFE TMGQEEKKTL NIVLKTDVRG
SLEALQGSLS SLGNDEVQVR VIGGGVGGIT ESDANLALAS NAVLFGFNVR ADAGARKIVE
QEGLDMRYYN VIYDIIEDVK KALTGMLGSD VRENILGVAE VRDVFRSPKF GAIAGCMVIE
GTVYRNRPIR VLREDVVIFE GELESLRRFK DDASEVRNGM ECGIGVKSYN DVKVGDKIEV
FEKVQVARTL
