ID IF2_CAMC1 Reviewed; 885 AA. AC A7ZC69; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 27-MAR-2024, entry version 94. 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=Ccon26_04760; ORFNames=CCC13826_1495; OS Campylobacter concisus (strain 13826). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360104; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=13826; RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., RA Mandrell R.E., On S., Nelson K.E.; RT "Genome sequence of Campylobacter concisus 13826 isolated from human RT feces."; RL Submitted (OCT-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}. 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; CP000792; EAT99040.1; -; Genomic_DNA. DR RefSeq; WP_012001357.1; NC_009802.2. DR AlphaFoldDB; A7ZC69; -. DR SMR; A7ZC69; -. DR STRING; 360104.CCC13826_1495; -. DR KEGG; cco:CCC13826_1495; -. DR eggNOG; COG0532; Bacteria. DR HOGENOM; CLU_006301_4_1_7; -. DR OrthoDB; 9811804at2; -. DR Proteomes; UP000001121; 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. FT CHAIN 1..885 FT /note="Translation initiation factor IF-2" FT /id="PRO_1000008219" FT DOMAIN 384..553 FT /note="tr-type G" FT REGION 55..150 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 269..300 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 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 885 AA; 96941 MW; 8A1AADE7F6978261 CRC64; MSNVRISEIA NELGYPSKEI VEKAQELGLK VKTHSNAVSL EEAEAIYEYV QTGVIPDKFK KKKSEPKAKK EPKKETEKEP AKKEEKPKTE PKKAATKAEP KPEKAKAEPK KEAQISEEKP KTEPKKEEPV KVEQKPAEAP KPKESLADVT QKRRGLVIVK KKKDYEAPAP IKEEKKAEAA VTNISDFKSM FSASDENLAR KKKKEKKVTV VSKKDSAEKM DLLGGSDFGD IVLEDEDVVV LPDFSFKTPA PTPMQRTKQP NAMKTTVNNT INSFGEGGIQ RRARKKHKKP ENKQNSEAVT SINIPKEIRV YEFAEKLNKQ PSEVIGKLFM LGMMTTKNDF LDEDAIEILA DEFNVEVNII DDQKEFDYVA AYEEEIKDDE NLQPRAPVIT IMGHVDHGKT SLLDYIRKSR VAAGEAGGIT QHVGAYMVNK NGRNITFIDT PGHEAFTAMR ARGAGVTDIV IIVVAADDGV KPQTKEAVSH AKAAGVPIII AINKMDKESA NPDLVKTGLA ELDIMPTEWG GKYEFVPISA KTGMGIDDLL EIVLLQADLL ELKANPKANA KATVIESSLQ KGRGPVATII VENGTLHVGD TVVAGVAYGK IRSLLDDQGR SLREIKPGEC GVIVGLSEIA EAGETLIGVK TDKEAREYAQ KKAEYIRQKE LSKSTKVSID ELSAKIAEGE LKTLPVIIKA DVGGSLEALK ASLEKLANDE IRVNVIHSGV GGITQSDVAL ASASNDCIIL GFNIRPTGEI KEKAKESGVE IKTYNVIYNL IDDVKAILGG LMSPIIREEQ LGQAQVRQVI HVPKVGTIAG CIVTEGTINR GAKIRLIREG VVVYEGLVSS LKRFKDDVKE VAKGYECGVG IENFNDIREN DYIESFKEVK EKATL //