IF2_PSEMY
ID IF2_PSEMY Reviewed; 828 AA.
AC A4XYE0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Pmen_3608;
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ymp;
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., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-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; CP000680; ABP86356.1; -; Genomic_DNA.
DR RefSeq; WP_003240571.1; NC_009439.1.
DR AlphaFoldDB; A4XYE0; -.
DR SMR; A4XYE0; -.
DR STRING; 399739.Pmen_3608; -.
DR PRIDE; A4XYE0; -.
DR EnsemblBacteria; ABP86356; ABP86356; Pmen_3608.
DR KEGG; pmy:Pmen_3608; -.
DR PATRIC; fig|399739.8.peg.3657; -.
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..828
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008305"
FT DOMAIN 328..501
FT /note="tr-type G"
FT REGION 93..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..344
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 362..366
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 383..386
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 437..440
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 473..475
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 93..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 337..344
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 383..387
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 437..440
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 828 AA; 89825 MW; 0A21308A7747C7BE CRC64;
MTQVTVKELA KVVDTPVERL LQQMREAGLS HDNAEQVVTD SEKQALLAHL KSSHGDKVEE
PRKITLQRKT TSTLRVAGSK TISVEVRKKK TFVKRSPEEL EAEKQRELEA QRAEAEAERL
KAEEEAKRKA EEEAKRQAAA ATSEAPAPAA SPAPLSEPVV AAPVVEVERK KEEVRRPEKA
RSDEDERRDR KHAQHRPTLK EKAPAPRVAP RSVDEESDGF RRGGRGKAKM KKRNQHGFQA
PAGPVVRDVA IGETITVADL AQQMSIKAAE VIKFMFKMGT PVTINQVLDQ ETAQLVAEEF
GHKVKLVSDN ALEEQLAESL KFEGEAMSRA PVVTVMGHVD HGKTSLLDYI RRAKVASGEA
GGITQHIGAY HVETDRGMVT FLDTPGHAAF TAMRARGAKA TDIVILVVAA DDGVMPQTQE
AVQHAKAAGV PIVVAVNKMD KPEANPDNIK NGLAALDVIP EEWGGDAPFV PVSAKAGTGI
DELLEAVLLQ AEVLELKATP TAPGRGVVVE SRLDKGRGPV ATVLVQDGTL RQGDMVLVGV
NYGRVRAMLD ENGKPIKEAG PSIPVEILGL DGTPDAGDEM MVVADEKKAR EVALFRQGKF
REVKLARAHA GKLENIFESM GQEEKKTLNI VLKADVRGSL EALQGSLSTL GNDEVQVRVV
GGGVGGITES DANLALASNA VLFGFNVRAD AGARKIVESE GLDMRYYNVI YDIIEDVKKA
LTGMLGSDVR ENILGTAEVR DVFRSPKFGA VAGCMVIEGT VYRNRPIRVL REDVVIFEGE
LESLRRFKDD VAEVRNGMEC GIGVKSYNDV KVGDKIEVFE KVQVARSL
