IF2_RHIEC
ID IF2_RHIEC Reviewed; 916 AA.
AC Q2KDZ5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=RHE_CH00116;
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251;
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(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; CP000133; ABC88941.1; -; Genomic_DNA.
DR RefSeq; WP_011423511.1; NC_007761.1.
DR AlphaFoldDB; Q2KDZ5; -.
DR SMR; Q2KDZ5; -.
DR STRING; 347834.RHE_CH00116; -.
DR EnsemblBacteria; ABC88941; ABC88941; RHE_CH00116.
DR KEGG; ret:RHE_CH00116; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_0_5; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001936; 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; Reference proteome.
FT CHAIN 1..916
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008311"
FT DOMAIN 414..581
FT /note="tr-type G"
FT REGION 1..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..430
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 448..452
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 469..472
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 523..526
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 559..561
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 423..430
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 469..473
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 523..526
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 916 AA; 99078 MW; 7FBBC0ED6ADAC3F9 CRC64;
MTDSNDDKTL SVTGKKTLTL KPSGMSQGTV RQDMGRGRTK AVVVETRKRR PMRPEDEKPI
TPATPAAPVR AAEPAPAPAQ ARPQQSTPAP RIHQPGGQAN QRPQQSYQPP RANDRPRPVV
LNHLSPEEMD ARRRALAESQ ARDAQDAIRR AEEEKRRAAE EAVRKAAEAE EAARRAVEEA
ARQAEAAAAA AAEPAVTAPA PAPVTAEARP NTSPRPAAPA PAARRPDADG AAARPAPGAP
AAVRGRRNDG DDDDRGASRG GPARGRVVRP EPAKPVTTRP KTDEERRRGK LTITTADVDG
EDAGRSRSLS AMRRRQEKFR RSQVQETREK ISREVVLPET ITIQELSQRM SERAVDVIKY
LMKEGQMMKP GDVIDADLAE LIAGEFGHTV KRVSESDVEL GIFNIADVEG DRVSRPPVVT
IMGHVDHGKT SLLDAIRHAN VVAGEAGGIT QHIGAYQVEQ NGQKITFIDT PGHAAFTAMR
ARGAQATDIA ILVVAADDSV MPQTIESINH AKAAGVPIIV AINKIDKHEA DPQKVRNQLL
QHEVFVESMG GETLDVEVSA KTGKNLDKLL EAVLLQAEIL DLKANPNRTA EGTVIEAQLD
RGRGAVATVL VQNGTLKPGQ IIVAGDVWGR VRALVNDKGE HMKEAPPAMP VEVLGLSGTP
QAGDKFAVVE SESRAREISE YRQRLARDKA AARQSGQRGS LEQMMTQMQS TGIKEFPLVI
KGDVQGSIEA IAGALEKLGT DEVRARIVHL GAGGITESDI SLAEASNAAI IGFNVRANAQ
ARQFAERQGI EIRYYNIIYD LVDDVKAAMS GLLSPERRET FIGNAEILEV FNITKVGKVA
GCRVVEGKVE RGAGVRLIRN DVVVHEGKLK TLKRFKDEVS EVPMGQECGM AFENYEDMRV
GDVIECFRVE HITRTL
