IF2_CALS8
ID IF2_CALS8 Reviewed; 858 AA.
AC A4XL70;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Csac_2070;
OS Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T
OS 6331).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis; Caldicellulosiruptor.
OX NCBI_TaxID=351627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A.,
RA VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J.,
RA Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M.,
RA Kengen S.M.W., Richardson P.;
RT "Genome sequence of the thermophilic hydrogen-producing bacterium
RT Caldicellulosiruptor saccharolyticus DSM 8903.";
RL Submitted (APR-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}.
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DR EMBL; CP000679; ABP67655.1; -; Genomic_DNA.
DR RefSeq; WP_011917590.1; NC_009437.1.
DR AlphaFoldDB; A4XL70; -.
DR SMR; A4XL70; -.
DR STRING; 351627.Csac_2070; -.
DR PRIDE; A4XL70; -.
DR EnsemblBacteria; ABP67655; ABP67655; Csac_2070.
DR KEGG; csc:Csac_2070; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 73560at2; -.
DR Proteomes; UP000000256; 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; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00487; IF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
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..858
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335461"
FT DOMAIN 361..530
FT /note="tr-type G"
FT REGION 59..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..377
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 395..399
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 416..419
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 470..473
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 506..508
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 370..377
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 416..420
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 470..473
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 858 AA; 96947 MW; F26DF4FC438CCE3D CRC64;
MTNKLRIYEF AKLLEIQNKD LMDILNKLNI EHKNHMSALE ENDINLVLEY ILQEKEKEKE
HAEKRRERLP SHKEGRSGER QAKTFDEKKH TRHGEKASHP YDKRGEQKLQ QKSQQDVRQK
FDREKRERHQ EAIAKESGKK LEGQERKAVV HDQKVVELFP QQEPEKRQAA KPKYEVAKEQ
KIEKRYQDKV AAKQKTEKAT KHRKQLFNVD ELTQEEVTVD REELEKIDKE VEDTLLEEEY
LQEKHVRRGK KEKLKKRSKE QKEVLKLQTK TVQEEKKEEI VKIPEKITVG EFANLIGKPA
AEVIKKLIML GVMANINQEI DFDVASLIAE DYGFKVEKEI IKSEEEILLE DQEDPEETLQ
PRPPVVVVMG HVDHGKTSLL DAIRNTNVTE KEAGGITQHI GASVVEVNGR KITFLDTPGH
EAFTAMRARG AQVTDIAVLV VAADDGVMPQ TVEAINHAKA ANVTIIVAIN KIDKPEANPE
RVKQQLSEYG LIPEEWGGDT VFVNVSAKKK IGIDHLLEMI LLVADLLELK ANPNRPARGR
VIEAKLDKGR GPVATVLVQK GTLKVGDYVV VGSTWGRVRA MIDDKGQRIK EAGPSMPVEI
LGLEDVPTAG DELVCVKDEK TAKTIAQIRQ ERLKEEKMQQ SKISLDELFE RIQKGQLKEL
RVIIKADVQG SVEALKSAIE RLSNDKVTVK VIHAAVGAIT ESDVTLASAS DAIIIGFNVR
PEVGAMSLAE KEKVDIRMYR IIYDVINDIK AAMKGLLEPV YKEVIIGHAE VRQIFKSSSV
GTIAGCYVLD GKITRTSNAR IIRDGVVVYE GKLASLKRFK DDVREVAAGY ECGMTFEKFN
DIKEGDIVEA FEMQKVES
