IF2_PSEU5
ID IF2_PSEU5 Reviewed; 837 AA.
AC A4VPP0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=PST_3310;
OS Pseudomonas stutzeri (strain A1501).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=379731;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1501;
RX PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT "Nitrogen fixation island and rhizosphere competence traits in the genome
RT of root-associated Pseudomonas stutzeri A1501.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
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; CP000304; ABP80941.1; -; Genomic_DNA.
DR RefSeq; WP_011914372.1; NC_009434.1.
DR AlphaFoldDB; A4VPP0; -.
DR SMR; A4VPP0; -.
DR STRING; 379731.PST_3310; -.
DR PRIDE; A4VPP0; -.
DR EnsemblBacteria; ABP80941; ABP80941; PST_3310.
DR GeneID; 66822707; -.
DR KEGG; psa:PST_3310; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_1_6; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000000233; 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; Reference proteome.
FT CHAIN 1..837
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008307"
FT DOMAIN 337..504
FT /note="tr-type G"
FT REGION 97..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 97..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..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; 90460 MW; 78BB864E323BC9D4 CRC64;
MTQVTVKELA QVVDTPVERL LQQMREAGLS HTSAEQVVTD NEKQALLAHL KSSHGAKVDE
PRKITLQRKT TTKLKVGGSK TISVEVRKKK TFVKRSAEEI EAEQRRELEE QRAAEEAARL
KAEQEARERA EEEARRQAEA AKAQTAETAA PAAAESASSA EPAQVVAAVE AAAPAPERKK
EEPRRVEKPR SDDDERRDRK HAQHRPSLKT KAPLARTVRS GEDEADGFRR GGRGGKSKLK
KRNQHGFQSP TGPVVREVSI GETITVAELA QQMSVKAAEV IKFMFKMGSP VTINQVLDQE
TAQLVAEELG HKVKLVSDNA LEEQLAELLK FEGESVARAP VVTVMGHVDH GKTSLLDYIR
RAKVAVGEAG GITQHIGAYH VETERGMVTF LDTPGHAAFT AMRARGAKAT DIVILVVAAD
DGVMPQTQEA VQHAKAAGVP IVVAVNKIDK PEANPDNIKN GLAALDVIPE EWGGDTPFIP
VSAKVGTGVD ELLEAVLLQA EILELKATPS APGRGVVVES RLDKGRGPVA TVLVQDGTLR
QGDMVLCGVN FGRVRAMLDE NGKPVKEAGP AIPVEILGLD GTPEAGDDLT VVADEKKARE
VALFRQGKFR EVKLARAHAG KLENIFETMG QDEKKTLNIV LKADVRGSLE ALQGSLNGLG
NDEVQVRVVG GGVGGITESD ANLALASNAV LFGFNVRADA GARKIVEAEG LDMRYYNVIY
DIIEDVKKAL TGMLGSDVRE NILGIAEVRD VFRSPKFGAI AGCMVTEGMV HRNRPIRVLR
DDVVIFEGEL ESLRRFKDDV AEVRAGMECG IGVKSYNDVK VGDKIEVFEK VEVARSL
