IF2_CHESB
ID IF2_CHESB Reviewed; 856 AA.
AC Q11BC8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Meso_3930;
OS Chelativorans sp. (strain BNC1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Chelativorans; unclassified Chelativorans.
OX NCBI_TaxID=266779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BNC1;
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 Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of chromosome of Mesorhizobium sp. BNC1.";
RL Submitted (JUN-2006) 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; CP000390; ABG65297.1; -; Genomic_DNA.
DR RefSeq; WP_011583238.1; NC_008254.1.
DR AlphaFoldDB; Q11BC8; -.
DR SMR; Q11BC8; -.
DR STRING; 266779.Meso_3930; -.
DR PRIDE; Q11BC8; -.
DR EnsemblBacteria; ABG65297; ABG65297; Meso_3930.
DR KEGG; mes:Meso_3930; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_2_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
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; 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; 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.
FT CHAIN 1..856
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008269"
FT DOMAIN 354..521
FT /note="tr-type G"
FT REGION 24..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..370
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 388..392
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 409..412
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 463..466
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 499..501
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 24..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..88
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 363..370
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 409..413
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 463..466
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 856 AA; 94136 MW; 72D83C873FB75FBB CRC64;
MTDTKTGDDK TLSVNTKKTL TIKRPGVEQG TVRQNFSHGR TKAVVVETKK RKFSRSDERV
EPVAPMRPKA PAPSPAPAPA PQPRETPRPQ PQQSRSGVVL NELSADEIEA RRRALQDAKL
RETEERKRAE EEARRRAEED ERRQREREES ARRQAEEEAR LKAEAEARKR AEEEAKRRTP
VVETPAVVAE AVEEEEERGG RGGLAKRGAV KPEAPVRPVK PRGEEERRRG KLTLNSALSD
EESTRSRSLS SMRRRQEKFK RAMQQEQREK VSREVVIPET ITIQELAQRM AERAVDVVKY
FMKQGQIMKP GDVIDADTAE LVAVEFGHTA KRVAESDVEE GLFNIEDRPE DLKPRPPVVT
IMGHVDHGKT SLLDAIRKAN VVAGEAGGIT QHIGAYQVEQ DGNTITFIDT PGHAAFTAMR
ARGAQATDIA ILVVAADDSV MPQTVESINH AKAAGVPIIV AINKIDKPDA NPQKVRTELL
QHEVFVESMG GDVLDVEVSA IKGTNLDKLL EAILLQAEIL ELKANPDRTA EGVVVEAKLD
RGRGSVATVL VQAGTLKPGD VIVAGSEWGR VRALVNERGE AVKVAPPSTP VEVLGLQGPP
QAGDRFAVVD TEARAREISE YRQRKAREKA VARQAGQRGS LEQMMSQLQS SGMKEFPLII
KGDVQGSIEA IVNALEKLGT EEVRARIVHS GAGAITESDI SLAETSDAAI IGFNVRANKQ
ARDAAEQAGI EIRYYNIIYD LVDDIKAAMS GLLSPERRET FLGNAEILEV FNITKVGKVA
GCRVTEGKVE RGAGVRLIRD NVVIHEGKLK TLKRFKDEVS EVPAGQECGM AFENYEDIRV
GDVIEAFRVE HVTRTL
