IF2_CLOB8
ID IF2_CLOB8 Reviewed; 695 AA.
AC A6LSQ4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Cbei_1202;
OS Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS acetobutylicum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=290402;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51743 / NCIMB 8052;
RG US DOE Joint Genome Institute;
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 Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA Blaschek H., Richardson P.;
RT "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL Submitted (JUN-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; CP000721; ABR33384.1; -; Genomic_DNA.
DR RefSeq; WP_011968539.1; NC_009617.1.
DR AlphaFoldDB; A6LSQ4; -.
DR SMR; A6LSQ4; -.
DR STRING; 290402.Cbei_1202; -.
DR EnsemblBacteria; ABR33384; ABR33384; Cbei_1202.
DR GeneID; 66344192; -.
DR KEGG; cbe:Cbei_1202; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000565; 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..695
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000075598"
FT DOMAIN 194..363
FT /note="tr-type G"
FT REGION 203..210
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 228..232
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 249..252
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 303..306
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 339..341
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 203..210
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 249..253
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 303..306
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 695 AA; 76128 MW; 3088C40F7DB0D354 CRC64;
MSKIRVHELA KELNIESKEL ITILKEEFNI EVKNHMSTIE DEDAELIKEL LAGKSPSDLV
ASADNAENSK SIVDVYEDEL AEQLNKGIKK KKKTKKEEQE EARIAAEAEA EGKVIEIGGS
ITVKELAEKL QQPSNDVIRT LIFAGVMAAI NAEIDFETAE KVCAEYGVLV ERKEEIQELE
VLKIEEDDEE NLQKRPPIVT VMGHVDHGKT SLLDCIRKAK VTDTEAGGIT QHIGAYTIKL
NGEEITFLDT PGHEAFTAMR ARGAQITDVV ILVVAADDGI MPQTKEAINH CKAAGVPIVV
AINKIDKPGA NVDRVKQELA EQGLLAEDWG GDTICEEVSA KQNLNIDKLL EMVLLTAEML
ELKANKDRRA VGTVIEAKLD KGRGAVASLL VQNGTLRVGD SILVGSTYGR IRAMFDDTGK
KIKSAGPSIP VEVLGLSEVP EAGDRFNQVK DEKTARNMAE SRKDKLKAET LLANHRVSLE
DLYNQIKEGK VKELAIIVKA DVQGSVEAIK QSLEKLSTDD VKVRVIHGGV GAITETDITL
ATASNAIVIG FNVRPDNNAA AQADRDGVDI KSYRIIYDAI DDVKSAMIGM LEPDYKEVIL
GTAEVRETYK ISNVGTIAGC YVLKGKLQRN AETRVIRDGI VIFESALSSL KRFKDDAKEV
NAGYECGLTI EKFNDIKEGD IVECFMMEAI KRKEL
