ID IF2_HALOH Reviewed; 686 AA.
AC B8CW72;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Hore_07840;
OS Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halothermotrichaceae;
OC Halothermothrix.
OX NCBI_TaxID=373903;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H 168 / OCM 544 / DSM 9562;
RX PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT "Genome analysis of the anaerobic thermohalophilic bacterium
RT Halothermothrix orenii.";
RL PLoS ONE 4:E4192-E4192(2009).
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; CP001098; ACL69541.1; -; Genomic_DNA.
DR RefSeq; WP_012635729.1; NC_011899.1.
DR AlphaFoldDB; B8CW72; -.
DR SMR; B8CW72; -.
DR STRING; 373903.Hore_07840; -.
DR KEGG; hor:Hore_07840; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000000719; 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 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..686
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000202776"
FT DOMAIN 186..355
FT /note="tr-type G"
FT REGION 35..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..202
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 220..224
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 241..244
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 295..298
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 331..333
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 45..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 195..202
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 241..245
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 295..298
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 686 AA; 75987 MW; F1908A3C4637AAF5 CRC64;
MSKIRVYKLA KELGKSSKEL VNILNDLGVE VSSHMSTVED ETAELVKGML QEEDKPEEKI
SKKEPDKKDR KKTKGKKQMT RTATQKEGTE HGQKDTDRRE MRVTVNPPLS VKELAEKADI
PVNRIIKTLI GLGVMATVNH QIDEEIVKKL IDKMNLKIKI SQGEDKEEKP DKVQTDIKDK
PEDLELRPPI VTVMGHVDHG KTTLLDVIRE TRVAESEAGG ITQHIGAYQA VVQNKKITFI
DTPGHEAFTA MRARGARLTD IAILVVAADD GVMPQTVEAI NHAKAADIPI IVAINKVDKS
NAQPDMVKQQ LTEHGLVPED WGGDTICVPI SALKKKNIDE LLEMVLLVAE MEELKANPDR
PAEGVIVESQ LDKGRGPVAT VLVKNGTLKV GDPILAGYTH GKVRAMINDQ GKRIKEALPS
TPVEVLGFSD VPAAGDYVQV LEDEKEARAI AEERLQKKQE RDLQHDGRIS LDGLYQQIKE
GGVKELNLII KGDVHGSIEA LRESLVKLST DEVTVNIIHT GVGAINETDV NLASASNAII
IGFNVRPDSN ARKLAEREKV EIKTYRVIYK IIEDLKDAMA GMLEPELKEE VTGRAEVRAT
FKVPNVGTVA GLYVKEGFIN RNNKVRLLRD GVVVYEGDIA SLKRFKNDVR EVKEGYECGL
GIEGYNDIKE GDQIETYTYR EIKRTL
//
