ID IF2_ALIB4 Reviewed; 890 AA. AC A8EWD7; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 1. DT 27-MAR-2024, entry version 98. 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=Abu_2043; OS Aliarcobacter butzleri (strain RM4018) (Arcobacter butzleri). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Arcobacteraceae; Aliarcobacter. OX NCBI_TaxID=367737; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RM4018; RX PubMed=18159241; DOI=10.1371/journal.pone.0001358; RA Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M., RA Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A., RA Rogosin A., Stanker L.H., Mandrell R.E.; RT "The complete genome sequence and analysis of the Epsilonproteobacterium RT Arcobacter butzleri."; RL PLoS ONE 2:E1358-E1358(2007). 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; CP000361; ABV68260.1; -; Genomic_DNA. DR RefSeq; WP_012147925.1; NC_009850.1. DR AlphaFoldDB; A8EWD7; -. DR SMR; A8EWD7; -. DR STRING; 367737.Abu_2043; -. DR KEGG; abu:Abu_2043; -. DR eggNOG; COG0532; Bacteria. DR HOGENOM; CLU_006301_4_1_7; -. DR Proteomes; UP000001136; 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; 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; 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..890 FT /note="Translation initiation factor IF-2" FT /id="PRO_0000335455" FT DOMAIN 387..554 FT /note="tr-type G" FT REGION 110..216 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 396..403 FT /note="G1" FT /evidence="ECO:0000250" FT REGION 421..425 FT /note="G2" FT /evidence="ECO:0000250" FT REGION 442..445 FT /note="G3" FT /evidence="ECO:0000250" FT REGION 496..499 FT /note="G4" FT /evidence="ECO:0000250" FT REGION 532..534 FT /note="G5" FT /evidence="ECO:0000250" FT COMPBIAS 110..133 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 145..160 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 176..216 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 396..403 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100" FT BINDING 442..446 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100" FT BINDING 496..499 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100" SQ SEQUENCE 890 AA; 97262 MW; 59D97729EA9DF258 CRC64; MSDTVRVYEI AEEAGASSQD VIAKAKDLGI ELKSPQTAVS YEDAEEITKY MMTGKSERLA TKPAKVKKVV KKEEVKKETE EIETPKEKIE TVQKVEKEII KKPELKKVEI SKPISKAPQK SEEESENLEN PNKIVPKRKG LVIIKKKRPK EEELEEQQTI TENQSKKQMK SLSEILGGVD DEEKSYNEPK NKENDDIKKQ KVKKEKKKPL IKTQDHGKKL DVDREYSDEF ASSDDSLLGE EIVLLDMDLS DSYKIFDEPK PQNIVNQSRS SKPAAFGNVP QGLKRGKRKK RIVRTQEKAE ITSVTIPEDI RVYEFAEACG KSPAEVITVL FSLGMMVTKN DFLKQDELEI LGEEFGIEVT VKDALEDVNY VETYNDEEDI DTSSFVTRPP VVTIMGHVDH GKTSLLDKIR SSKVAAGEAG GITQHITSYT VTKNGQEITF VDTPGHAAFS AMRARGANVT DIIIIVVAAD DGVKMQTEEV ISHAKASGCP IIVAMNKMDK ETANPDMVKA QMAEKGLTPI DWGGDIEFIG VSARTGDGIE DLLENILLQA EILELKADPT AKAKATVIEA SLEKGRGPVA NVIVQNGTLK IGDNIVCDTT FGRVKAITDD NGKPVKELGL SQTGTVLGLN EVPTTGSVLV AMDTEKEVRE IATTRAEHAR AKELSKSTKV SLEEMSGLIA EGKIKQLPVI IKADVGGSLE AIKGSLEKIA NDEVKVKVVH AAVGGITESD LVLAGASGEC IILGFNVRPT GSVKAKAKAD GVTINTYSII YDLIDDVKHA LSGMMSAVIR EENTGQAEVR DTFVVPKVGT VAGCLVTDGK VIRGGHARII RDGVVTYTGK ISSLKRFKDD VKEVANGYEC GIMFDKFNDI KVGDFIETFI QIEEKVSVDD //