IF2_LEIXX
ID IF2_LEIXX Reviewed; 916 AA.
AC Q6AG49;
DT 02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Lxx07150;
OS Leifsonia xyli subsp. xyli (strain CTCB07).
OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Leifsonia.
OX NCBI_TaxID=281090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CTCB07;
RX PubMed=15305603; DOI=10.1094/mpmi.2004.17.8.827;
RA Monteiro-Vitorello C.B., Camargo L.E.A., Van Sluys M.A., Kitajima J.P.,
RA Truffi D., do Amaral A.M., Harakava R., de Oliveira J.C.F., Wood D.,
RA de Oliveira M.C., Miyaki C.Y., Takita M.A., da Silva A.C.R., Furlan L.R.,
RA Carraro D.M., Camarotte G., Almeida N.F. Jr., Carrer H., Coutinho L.L.,
RA El-Dorry H.A., Ferro M.I.T., Gagliardi P.R., Giglioti E., Goldman M.H.S.,
RA Goldman G.H., Kimura E.T., Ferro E.S., Kuramae E.E., Lemos E.G.M.,
RA Lemos M.V.F., Mauro S.M.Z., Machado M.A., Marino C.L., Menck C.F.,
RA Nunes L.R., Oliveira R.C., Pereira G.G., Siqueira W., de Souza A.A.,
RA Tsai S.M., Zanca A.S., Simpson A.J.G., Brumbley S.M., Setubal J.C.;
RT "The genome sequence of the Gram-positive sugarcane pathogen Leifsonia xyli
RT subsp. xyli.";
RL Mol. Plant Microbe Interact. 17:827-836(2004).
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; AE016822; AAT88646.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6AG49; -.
DR SMR; Q6AG49; -.
DR STRING; 281090.Lxx07150; -.
DR EnsemblBacteria; AAT88646; AAT88646; Lxx07150.
DR KEGG; lxx:Lxx07150; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_1_11; -.
DR OMA; QVRPEMI; -.
DR Proteomes; UP000001306; 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.
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..916
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137214"
FT DOMAIN 409..583
FT /note="tr-type G"
FT REGION 58..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..425
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 443..447
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 468..471
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 522..525
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 558..560
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 157..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..210
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 418..425
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 468..472
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 522..525
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 916 AA; 95933 MW; 3FF1147671FAA2CA CRC64;
MGPDRRIVAA KPRVHEVASE LGVDSKIALA KLKEMGEFVK GPSSSIEPPV ARKLRAALEA
EGHLPGAGGD KTAAQASPAP RPPRPATADG SGAPKPQAPM SVAERQAAAE KAASEKAAAE
KVAASEAADA KPAAGAPADT AKPSSPPRPS GVSAPRPGNN PFASNQGMGQ RPSAPRPGNN
PFSSSQGMGQ RPSPSNIPRP APPRPGSPRI GAPRPGGGQR QGGGGRPGFQ QRPGSAGGGA
GGGLQRPGGA GAGGFSGPRT GGGGGRGRGP GGGTAGAFGR GGGKSKARKS KRAKRQEFEM
REAPSLGGVT VPRGDGGTAI RLRRGASISD FADKIDANPA SLVTVLFHLG EMATATESLD
EATFQILGEE LGYKVQVVSP EDEDKELLEG FDIDLDAELE GESDEDLEIR PPVVTVMGHV
DHGKTRLLDA IRSANVVEGE AGGITQHIGA YQVWTEHEGI ERAITFIDTP GHEAFTAMRA
RGAQVTDIAI LVVAADDGIM PQTIEALNHA QAANVPIVVA VNKVDKPEAN PAKVRQQLTE
FSLVAEEYGG DVMFVDVSAR NNIGIQELLD AVLLTADAGL DLRANPNKDA RGVAIEAKLD
KGRGAVATVL IQSGTLRVGD AIVAGTAYGR VRAMADENGD PVLEAAPSRP VQVQGLSSVP
RAGDTFIVTE EDRTARQIAE KREAAERNAQ LAKARKRISL EDFTRALEEG KVEALNLIIK
GDVSGAVEAL EESLMKIEVD DSVSLRILHR GVGAITESDI DLATIDNAIV IGFNVRPDVK
ARERAAREGV DVRFYSVIYN AIDDIESSLK GMLKPEFEEV QSGVADIREV FRSSKFGNIA
GVIVRSGTIT RNAKARVIRD GVVIADNLAI ESLRRFKDDV TEVRTDFECG IGLGKYNDIQ
VGDEIETIEM REKPRV
