ID IF2_HELP2 Reviewed; 947 AA. AC B6JKX5; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 1. DT 27-MAR-2024, entry version 81. DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100}; GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; GN OrderedLocusNames=HPP12_0396; OS Helicobacter pylori (strain P12). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=570508; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P12; RA Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.; RT "The complete genome sequence of Helicobacter pylori strain P12."; RL Submitted (OCT-2008) 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; CP001217; ACJ07553.1; -; Genomic_DNA. DR RefSeq; WP_001293382.1; NC_011498.1. DR AlphaFoldDB; B6JKX5; -. DR SMR; B6JKX5; -. DR KEGG; hpp:HPP12_0396; -. DR HOGENOM; CLU_006301_4_0_7; -. DR Proteomes; UP000008198; 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; 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; 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; PF11987; IF-2; 1. DR Pfam; PF04760; IF2_N; 1. 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. FT CHAIN 1..947 FT /note="Translation initiation factor IF-2" FT /id="PRO_1000093791" FT DOMAIN 446..615 FT /note="tr-type G" FT REGION 61..284 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 455..462 FT /note="G1" FT /evidence="ECO:0000250" FT REGION 480..484 FT /note="G2" FT /evidence="ECO:0000250" FT REGION 501..504 FT /note="G3" FT /evidence="ECO:0000250" FT REGION 555..558 FT /note="G4" FT /evidence="ECO:0000250" FT REGION 591..593 FT /note="G5" FT /evidence="ECO:0000250" FT COMPBIAS 91..121 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 151..165 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 166..190 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 191..232 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 248..267 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 455..462 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100" FT BINDING 501..505 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100" FT BINDING 555..558 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100" SQ SEQUENCE 947 AA; 105682 MW; FE2C4C36621F1DC4 CRC64; MSEMVDLKEF LAELGKTQKE LKNVIEQAKD IGLELKTNSK MTPEQAGKLY KYIVDGIKEQ IQANQPAKNP EQDNKDDLNT AVASKSLNKK VFKTPKKEET KSQPKPKKTK EKKKEAPTPI AKKKGGIEIV NTFEDQTPPV ENAPKVVSHS QIEKAKQKLQ EIQKSREALN KLTQSNANNA NSTNNANNAK KEISEVKKQE QEIKRHENIK RRTGFRVIKR NDETENETEN SVTESKKPTQ SAAAIFEDIK KEWQEKDKQE AKKVKKPSKP KATPTAKNNK SHKIDFSDAR DFKGNDIYDD ETDEILLFDL HEQDNLNKEE EEKEIRQNIN DRVRVQRKNP WMNESGIKRQ SKKKRAFRND NSQKVIQSAI AIPEEVRVYE FAQKANLNLA DVIKTLFNLG LMVTKNDFLD KDSIEILAEE FHLEISVQNT LEEFEVEEVL EGVKKERPPV VTIMGHVDHG KTSLLDKIRD KRVAHTEAGG ITQHIGAYMV EKNNKWVSFI DTPGHEAFSQ MRNRGAQVTD IAVIVIAADD GVKQQTIEAL EHAKAANVPV IFAMNKMDKP NVNPDKLKAE CAELGYNPVD WGGEHEFIPV SAKTGDGIDN LLETILIQAD IMELKAIEEG SARAVVLEGS VEKGRGAVAT VIVQSGTLSV GDSFFAETAF GKVRTMTDDQ GKSIQNLKPS MVALITGLSE VPPAGSVLIG VENDSIARLQ AQKRATYLHQ KALSKSTKVS FDELSEMVAN KELKNIPVVI KADTQGSLEA IKNSLLELNN EEVAIQVIHS GVGGITENDL SLVSNSEHAV ILGFNIRPTG NVKNKAKEYN VSIKTYTVIY ALIEEMRSLL LGLMSPIIEE EHTGQAEVRE TFNIPKVGTI AGCVVSDGVI ARGIKARLIR DGVVIHTGEI LSLKRFKDDV KEVSKGYECG IMLDNYNEIK VGDVFETYKE IHKKRTL //