ID IF2_ACIC1 Reviewed; 879 AA.
AC A0LV27;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Acel_1515;
OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae;
OC Acidothermus.
OX NCBI_TaxID=351607;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43068 / DSM 8971 / 11B;
RX PubMed=19270083; DOI=10.1101/gr.084848.108;
RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT "Complete genome of the cellulolytic thermophile Acidothermus
RT cellulolyticus 11B provides insights into its ecophysiological and
RT evolutionary adaptations.";
RL Genome Res. 19:1033-1043(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; CP000481; ABK53287.1; -; Genomic_DNA.
DR RefSeq; WP_011720350.1; NC_008578.1.
DR AlphaFoldDB; A0LV27; -.
DR SMR; A0LV27; -.
DR STRING; 351607.Acel_1515; -.
DR KEGG; ace:Acel_1515; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_3_11; -.
DR InParanoid; A0LV27; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000008221; 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 PRINTS; PR00315; ELONGATNFCT.
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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..879
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008188"
FT DOMAIN 372..543
FT /note="tr-type G"
FT REGION 48..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..388
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 406..410
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 431..434
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 485..488
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 521..523
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 64..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..197
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 381..388
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 431..435
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 485..488
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 879 AA; 92534 MW; 2AF7D619B8ACDEAE CRC64;
MAKVRVYELA KELNVESKTL LAKLHELGEF VRSASSTIEA PVVRKLREAF PPPPEPAAGN
GSAAQPTAKP SAAKSTGKTT EPAADAAAPP AVTTPPSAAP AGATTSAPSD AGGEKIATPP
RPVKLPQPPR PAPAVPKPPS GPPRMGNNPF TSPMPRPMPP RPVQRPTGTP GTPGIPRPPL
RPGAPGRPTP GAMPPRPAAG RAAPGRGAPI RLPGGLGRAP APPSAGRPGV GGRGRGAPGG
AFGRGPGAKP SRPHKSKKQR RQEFDNLQAP VIGGIQIPRG NGQVVRLPRG ASLADFADKI
GANPASLVQV AFHLGEMVTA TQSVNEETLQ LLGAELGYEV QIVSPEDEDR ELLESFDIEL
GTDQGDEAAL VPRPPVVTVM GHVDHGKTKL LDAIRNTNVA AREHGGITQH IGAYQVTAQT
ADGPRQITFI DTPGHEAFTA MRARGAQVTD IAVLVVAADD GVMPQTVEAL NHAKAADVPI
VVAVNKIDKP GADPVKVRGQ LTEYGLVAEE YGGDTMFVDV SALTGQGIDD LLEAILLTAD
AALDLRANPN QPAQGVAIEA HLDRGRGPVA TVLVQRGTLR VGDSIVAGEA FGRVRAMLDE
FGQPVEEAGP SRPVQVLGFT SVPDAGDTFL VVPEDRVARQ IAERRAARER NAQLAASRRR
RTLEDILERM EKGEVAELRL ILKGDVSGSV EALEDALLKI DVGDEARIRV IDRGVGAITE
NNVMLAVASD AIIIGFNVRP EGKARELAER EGVDVRYYSV IYQAIEDVEA ALKGLLKPVY
EEVQLGTAEV REVFRSSKFG NIAGCLVRSG TITRGAKARV VRDGVVVAND VSIASLRRFK
DDVTEVREGF ECGVGLGSFN DIRVGDVIET YEMREKPRS
//
