IF2_RHIL3
ID IF2_RHIL3 Reviewed; 917 AA.
AC Q1MN39;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=RL0125;
OS Rhizobium leguminosarum bv. viciae (strain 3841).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=216596;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3841;
RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT components.";
RL Genome Biol. 7:R34.1-R34.20(2006).
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; AM236080; CAK05613.1; -; Genomic_DNA.
DR RefSeq; WP_011649946.1; NC_008380.1.
DR AlphaFoldDB; Q1MN39; -.
DR SMR; Q1MN39; -.
DR STRING; 216596.RL0125; -.
DR EnsemblBacteria; CAK05613; CAK05613; RL0125.
DR KEGG; rle:RL0125; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_0_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000006575; 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; 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..917
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008312"
FT DOMAIN 415..582
FT /note="tr-type G"
FT REGION 1..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..431
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 449..453
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 470..473
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 524..527
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 560..562
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 38..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 424..431
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 470..474
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 524..527
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 917 AA; 99537 MW; F143241E4F66E5D8 CRC64;
MTDSNDDKTI SVAGKKTLTL KPSGMSQGTV RQDMGRGRTK AVVVETRKRR PMRPEDEKPI
TPVAPAAPVR AAEPAPAPVQ ARPQQPTPAP RVQQGNNNQT NQRPPQQSHQ PPRQNDRPRP
VVLNHLSPEE MDARRRALAD SQARDAQDAI RRAEEEKRRA AEEVIRKAAE AEEAARRAAE
EAIRQAEAPA VAEPAAAEPA PAEARTDAPR PPQPASSAPA ARRPDAAGAP AARPAPGAAV
PGAVRGRRDE KEEDDRGAAR GGPVRGRVVR PEPAKPVTTR PKTDEERRRG KLTITTANVD
GEDNARGRSL SAMRRRQEKF RRGQMQETRE KISREVVLPE TITIQELSQR MSERAVDVIK
YLMKEGQMMK PGDVIDADLA EIIAGEFGHT VRRVSESDVE LGIFNVSDED GELVSRPPVV
TIMGHVDHGK TSLLDAIRHA NVVSGEAGGI TQHIGAYQVE QNGQKITFID TPGHAAFTAM
RARGAQATDI AILVVAADDS VMPQTIESIN HAKAAGVPII VAINKVDKHE ADPQKVRNQL
LQHEVFVESM GGEVLDVEVS AKTGKNLDKL LEAILLQAEI LDLKANANRT AEGTVIEAQL
DRGRGSVATV LVQKGTLRPG QIIVAGDVWG RVRALVTDKG DHVKEAGPAT PVEVLGLSGT
PQAGDKFAVV ESESRAREIS EYRQRLARDK AAARQSGQRG SLEQMMMQRQ SVGIKEFPLV
IKGDVQGSIE AIAGALEKLG TDEVRARIVH SGAGGITESD ISLAEASNAA IIGFNVRANT
QARQFAEREG IEIRYYNIIY DLVDDVKAAM SGLLSPERRE TFIGNAEILE VFNITKVGKV
AGCRVVEGKV ERGAGVRLIR NDVVVHEGKL KTLKRFKDEV SEVPMGQECG MAFENYEDMR
AGDVIECFRV EHITRTL
