ID IF2_GEOUR Reviewed; 882 AA.
AC A5GF86;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, 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=Gura_1901;
OS Geotalea uraniireducens (strain Rf4) (Geobacter uraniireducens).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geotalea.
OX NCBI_TaxID=351605;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1134 / JCM 13001 / Rf4;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M.,
RA Lovley D., Richardson P.;
RT "Complete sequence of Geobacter uraniireducens Rf4.";
RL Submitted (MAY-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; CP000698; ABQ26091.1; -; Genomic_DNA.
DR RefSeq; WP_011938794.1; NC_009483.1.
DR AlphaFoldDB; A5GF86; -.
DR SMR; A5GF86; -.
DR STRING; 351605.Gura_1901; -.
DR KEGG; gur:Gura_1901; -.
DR HOGENOM; CLU_006301_10_0_7; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000006695; 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; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 1.10.10.2480; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR004161; EFTu-like_2.
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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
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..882
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335473"
FT DOMAIN 382..551
FT /note="tr-type G"
FT REGION 123..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..398
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 416..420
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 437..440
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 491..494
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 527..529
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 224..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 391..398
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 437..441
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 491..494
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 882 AA; 96150 MW; DCA5BA1C2AA50147 CRC64;
MSKTRVYELA QQMGIENKEL MSRLKAIGVE VSNHMAAIDD ADIKKLTAPA TVKEVSQEEV
RVKPTLIRRR AKVVETVAEE APEEVAVEAP PVKVVEAEIE KPEPVVVAAV EVAKPAPEEV
VKVERVEEPQ PEKPTANRAR ILGRMEIPGL KPKERPPVQR EAQRPAVAPS RAPERPAAKP
GTERPASQRY PDRPAPPRGT ERPSTSRVPE RVTPIVPLAV PPVGEERRKG RKGKEVAAGN
GKKGAAGVVV PKRKEEFKKT DLLEKHERIF EPGPRGKGKK RHVEKVSVGK KTEITVPKAI
KRIIKISETI TVGELAKRMG IKATDLIRAL MKMGVMATIN HPLDVDTATL LATEFGYEIE
NVALDIDEIL ESAPDALESL VKRPPVVTIM GHVDHGKTSL LDAIREANVI AGEAGGITQH
IGAYDVELNG RKITFLDTPG HEAFTAMRAR GAKVTDIVIL VVAADDGVMP QTREAVNHSK
AAGVPIIVAV NKIDKPEAKP ERVKQELMEL GLVSEEWGGD TIFVEVSAKK RINLPSLLEM
VLLQADVLEL KANPEKAARG TIVEAKLDKG RGPVATVLVQ EGTLKVGDYF VAGVHFGRVR
AMQNDRGDKV LSAGPSMPAE VIGFTGVPDA GDVFVALADE KQAKEIASLR QQKLRETELA
KHTKLSLEQL YEKIQMGEVK DLNVIVKGDV QGSVEAVAES LRKLSTDAIR LNVIHASVGA
ITETDVNLAT ASNAIILGFN VRPEVKAQAL AEKEGVDVRL YNIIYDAVDD IKKAMEGLLE
PTLREKFLGR AEIRETFSVP KHGTVAGSYV LDGKMVRNAQ VRLLRDNVVV YEGKMASLRR
FKDDVKDVAT GYECGISLEN YNDIKVGDII EAFEIEKIAT KL
//
