IF2_EDWI9
ID IF2_EDWI9 Reviewed; 901 AA.
AC C5BFB7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=NT01EI_0467;
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=634503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146;
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) 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; CP001600; ACR67703.1; -; Genomic_DNA.
DR RefSeq; WP_015869905.1; NC_012779.2.
DR AlphaFoldDB; C5BFB7; -.
DR SMR; C5BFB7; -.
DR STRING; 67780.B6E78_13095; -.
DR PRIDE; C5BFB7; -.
DR EnsemblBacteria; ACR67703; ACR67703; NT01EI_0467.
DR GeneID; 7961290; -.
DR KEGG; eic:NT01EI_0467; -.
DR PATRIC; fig|634503.3.peg.424; -.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001485; 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; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF46955; SSF46955; 1.
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; Reference proteome.
FT CHAIN 1..901
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000202771"
FT DOMAIN 400..569
FT /note="tr-type G"
FT REGION 48..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..416
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 434..438
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 455..458
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 509..512
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 545..547
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 61..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 409..416
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 455..459
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 509..512
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 901 AA; 98216 MW; 1AED0DB028854646 CRC64;
MAEVTVKSLA AEIQTSVERL VQQLADAGIN KSPDDSVSPQ EREALLAHLN REHGGSSDKL
TLQRKTRSTL SVPGTGGKSK SVQIEVRKKR TYVKSDAAAQ QAEAEALAKR EAEEQVKREA
EEQTQRDMAE LAKREAAEQA KRQQEEQAKR EAAEKAKREA AEKEKVTNQH IDEKTKAAQA
EKAKREAEAA ELKRKAEEEA RRKLEEDARK VAEEARRMAE ANEGKWTENA SEEDNSDYHV
TTSHHAREAE DENDRQVEGD RRARGRGGKA AKQKKGSKLS ESKADREEAR AVNRGGKGGK
RKPSSLQQGF TKPAQAVNRD VVIGETITVA ELANKMAVKG SQVIKAMMKM GAMATINQVI
DQETAQLVAE DMGHKVILRR ENELEEAVLS DRDTGAAAEP RAPVVTIMGH VDHGKTSLLD
YIRSTKVAAG EAGGITQHIG AYHVQTDNGM ITFLDTPGHA AFTAMRARGA QATDIVVLVV
AADDGVMPQT IEAVQHAKAA GVPLVVAVNK IDKPEADPDR VKNELSQYGV MPEEWGGEAQ
FVHVSAKAGT GIDELLDAIL LQAEVLELKA VRNGMASGVV IESFLDKGRG PVATVLVREG
TLNKGDIVLC GFEYGRVRAM RDELGREITE AGPSIPVEIL GMSGVPAAGD EATVVRDEKK
AREVALYRQG KFREVKLARQ QKAKLENMFS NMVEGEVSEL NIVLKADVQG SVEAIADSLR
KLSTDEVKVK IVGSGVGGIT ETDATLAAAS NAILLGFNVR ADASARRVVE AENLDLRYYS
VIYDLIDEVK QAMSGMLAPE YKQEIIGLAE VRDVFKSPKF GAIAGCMVTE GVVKRHSPIR
VLRENVVIYE GELESLRRFK DDVNEVRNGM ECGIGVKNYN DVRPGDVIEV FETIEVKRTI
D
