IF2_CORDI
ID IF2_CORDI Reviewed; 953 AA.
AC Q6NGN2;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=DIP1477;
OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS gravis).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=257309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX PubMed=14602910; DOI=10.1093/nar/gkg874;
RA Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA Parkhill J.;
RT "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT NCTC13129.";
RL Nucleic Acids Res. 31:6516-6523(2003).
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; BX248358; CAE50005.1; -; Genomic_DNA.
DR RefSeq; WP_010935094.1; NC_002935.2.
DR AlphaFoldDB; Q6NGN2; -.
DR SMR; Q6NGN2; -.
DR STRING; 257309.DIP1477; -.
DR EnsemblBacteria; CAE50005; CAE50005; DIP1477.
DR KEGG; cdi:DIP1477; -.
DR HOGENOM; CLU_006301_9_0_11; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002198; 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 PRINTS; PR00315; ELONGATNFCT.
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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..953
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228186"
FT DOMAIN 449..621
FT /note="tr-type G"
FT REGION 55..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..465
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 483..487
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 508..511
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 562..565
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 598..600
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 93..117
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 458..465
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 508..512
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 562..565
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 953 AA; 99597 MW; 8F8496388FE5F7FC CRC64;
MPGKLRVHEL AKQLGVTSKE LLATLKDQGE FVKTASSTIE PPVVKKMKKH YESLGVTTEA
PAASQEPKAK KPAAPKPAAP KPAATPQQAA KPAAPKPAAP KPAAEKKPAP KPAAKPVPKP
GFSAAKAESS APKPAAPKPA APKPAAQSST TATPGSMPRP QAKPAPKPGG RAPRVANNPF
SSGPRPAPRP GGGNRSGNAP RPGGGPRPGG NRPQGGQGGP AERAPRPGGR GGQPRPQGGS
RSQQSGGQER QGGGRRPSPA MMPTHPNPGQ MPSRSNGSRN GRGGAGGQGG RPGFGGGRPG
GGGSAGGRGG RRGGTAGAFG RPGGAPRKGR KSKRQKRNEY EAMQAPNVIG GVRLPDGGGA
TIRLARGASL SDFAEKINAD AAALVQALFN LGEMVTATAS VNEETLQLLG EEMNYKVEVV
SPEDEDRELL ESFDLQFGED EGTEEDLAKR PPVVTVMGHV DHGKTRLLDT IRKTNVGSDE
AGGITQGIGA YQVTVNIDDL SRKITFLDTP GHEAFTAMRA RGAKSTDIAV LVVAADDGVM
PQTVEAINHA KAADVPIVVA VNKIDKPGAS PDKIRGQLTE YGLVPEEYGG DTMFVDISAK
QNINIDGLLE AVLLTADASL DLRANPDMDA QGVAIEAHLD RGRGPVATVI VQRGTLRVGD
SVVAGDAYGR VRRMVDEYGN DVEEAGPSRP VQMQGLNGVP GAGDNLLVVE DDRVARQIAN
QRNARKRNAL AAKTRKRVSL EDLDSVLKET STLNLILKGD NAGSVEALED ALLKIEVDDE
VQLNIIDRGV GAVTQTNVSL AAASDAVIIA FNVRAEGKAT EEANAEGVDI RYYTVIYRAL
EEVEQALKGM LKPIYEEREI GRAEIRAIFK ASAVGLIAGC MVESGKVRRN ASIRLLRDGT
VVADNAKIES LRREKDDATE VAAGYECGMV LSYPDIQVGD IIEVFEQVEV PRT
