IF2_GEOMG
ID IF2_GEOMG Reviewed; 884 AA.
AC Q39VA6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Gmet_1586;
OS Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=269799;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Geobacter metallireducens GS-15.";
RL Submitted (OCT-2005) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000148; ABB31818.1; -; Genomic_DNA.
DR RefSeq; WP_011365850.1; NC_007517.1.
DR AlphaFoldDB; Q39VA6; -.
DR SMR; Q39VA6; -.
DR STRING; 269799.Gmet_1586; -.
DR EnsemblBacteria; ABB31818; ABB31818; Gmet_1586.
DR KEGG; gme:Gmet_1586; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_7; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 79180at2; -.
DR Proteomes; UP000007073; 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; 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; PF04760; IF2_N; 2.
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..884
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228200"
FT DOMAIN 384..553
FT /note="tr-type G"
FT REGION 42..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..400
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 418..422
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 439..442
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 493..496
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 529..531
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 192..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 393..400
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 439..443
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 493..496
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 884 AA; 96112 MW; EEAAB5E70414919D CRC64;
MSKTHVYELA KKMGVENKEL MARLKSLGIE VKSHLSVLED EDVQKVTAPP TPPKGVQQQE
EVRVTTTVIR RRPKAVAQPP EEVAPAAVES AVIEEAPAPR VEAVPEEPKA SPAFAETVPA
VEEPKGVEPK IGVPKVETPV ASESKAEEPR VTAPPAQPKP VAAEEEKPTM NRARILGRVE
LPGLTTASKP VPKPAERREV VIPPKRKMEE RAVTPQPAAP VADDRKKKAK TFTEPETPAG
GAPGAKKGAP GGKKKEAFKK AELLEKRERI FEPGPKTGKG RRRERESVTF GKKTEITVPK
AIKRIIKISE SITVGELAKR MGVKATDLIR VLMKMGMMAT INHPLDVDTA TLIAAEFSYE
IENVAIDTDE MLESAPDTPE SLKKRPPVVT IMGHVDHGKT SLLDAIREAN VIAGEAGGIT
QHIGAYDVEL NGRKITFLDT PGHEAFTAMR ARGAKVTDIV ILVVAADDGV MPQTREAINH
SKAAGVPIII AINKIDKPEA KPERVKQELM EFGLVSEEWG GETIFVEVSA KKRINLPELL
EMVLLQADVM DLKANPDKEA RGTIVEAKLD RGRGPVATVL VQEGTLKVGD YFVAGVHSGR
VRAMQNDRGD KVLAAGPSMP VEVIGFTGVP DAGDVFISLS DEKKAKEIAS HRQQKLRETE
LAKHSKMSLE QLYDKIQKGE VKDLNAIVKA DVQGSVEAVS DSLRKLSTDA VRLNVIHSSV
GAITETDVNL ASASNAIILG FNVRPEPKAS AMAEKEGVDV RLYNIIYDAV EDIKKAMEGL
LEPTLREKYL GRAEIREVFS VPKVGNVGGC YIQDGKVLRN ASVRLLRDNV VVYEGKMSSL
RRFKDDVKEV ATGYECGIGL ENYNDIKVGD IIEAFEIEKI ATKL
