IF2_CITBB
ID IF2_CITBB Reviewed; 986 AA.
AC B5EI57;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Gbem_1302;
OS Citrifermentans bemidjiense (strain ATCC BAA-1014 / DSM 16622 / JCM 12645 /
OS Bem) (Geobacter bemidjiensis).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Citrifermentans.
OX NCBI_TaxID=404380;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1014 / DSM 16622 / JCM 12645 / Bem;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Lovley D., Richardson P.;
RT "Complete sequence of Geobacter bemidjiensis BEM.";
RL Submitted (JUL-2008) 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; CP001124; ACH38321.1; -; Genomic_DNA.
DR RefSeq; WP_012529733.1; NC_011146.1.
DR AlphaFoldDB; B5EI57; -.
DR SMR; B5EI57; -.
DR STRING; 404380.Gbem_1302; -.
DR EnsemblBacteria; ACH38321; ACH38321; Gbem_1302.
DR KEGG; gbm:Gbem_1302; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_7; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 79180at2; -.
DR Proteomes; UP000008825; 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 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..986
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093788"
FT DOMAIN 486..653
FT /note="tr-type G"
FT REGION 47..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..502
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 520..524
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 541..544
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 595..598
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 631..633
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 56..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..291
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 495..502
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 541..545
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 595..598
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 986 AA; 105096 MW; 8F629DB3432EC416 CRC64;
MSKTRVYELA QQMGIDNKEL MARLADAGVS VKNHMAVLED SDIKALSAPA QTPHKEVSQE
EVRVKPTLIR RRAKAVEPEA ASAEAASAPA AQEEAPQKAE PEKVEAEKAE APKPRQAAEP
VRARIIEAAP VPKPAAAPAE AAKPEKAKPA EPAPVAAAPK AAEAPAAPAA EAAPAAPAPA
EAPVAKPAAK LEASAPAAPA APAAAAPVEA QAPAKAEEQE PEKATPTRAR ILGRVEIPIP
AQRPAERREY QRTAPGERPA PRPGMPRGVE RPGTERPAPR PGGPRPAGAP GRPGERPTTG
RPGGPTGGRP DRPAPLAPID APPLLGDDRR KGRKPAPAGG TDYAKNGKKG APAAAGKGKK
DSFKDILDKR ERVFEPGPRS KGRKGKYEKV QIGKKTEITV PKAIKRIIKI SESITVGELA
KRMGIKATDL IRALMKLGVM ATINHPLDFD TATLLATDFG YEIENVALDV DEILEAEPDT
PESLLKRPPV VTIMGHVDHG KTSLLDAIRE ANVIAGEAGG ITQHIGAYDV ELNGKKITFL
DTPGHEAFTA MRARGAKVTD IVILVVAADD GVMPQTREAV NHSKAAGVPI IVAINKIDKP
DASPGKVKQE LMEFGLVSEE WGGETIFVEV SAKKRINLES LLEMVLLQAD VLELRANPDK
PARGTIVEAK LDKGRGPVAT VLVQEGTLKS GDYFVAGVHY GRVRAMQNDR GEKVLAAGPA
MPVEVIGFNG VPDAGDIFVA MGDEKQAKEI ANHRQMKLRE SELAKHSKLS LEQLYEKIQK
GEVKDLNAIV KGDVQGSVEA VAESLRKLST DAIRLNVLHA SVGAITETDV NLASASNAII
LGFNVRPEVK AAALAEKEGV DVRLYNIIYD AVDDIKKAME GLLEPTFKEK YLGRAEIREV
FSVPKAGMVA GSYVTDGKIV RNAQVRLLRD NMVVYEGKLG SLRRFKDDVK EVATGYECGM
SLENYNDLKI GDIFECFEME KVAGKL
