IF2_GRABC
ID IF2_GRABC Reviewed; 915 AA.
AC Q0BPG2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=GbCGDNIH1_2392;
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1260 / CGDNIH1;
RX PubMed=17827295; DOI=10.1128/jb.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(2007).
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; CP000394; ABI63290.1; -; Genomic_DNA.
DR RefSeq; WP_011633092.1; NC_008343.2.
DR AlphaFoldDB; Q0BPG2; -.
DR SMR; Q0BPG2; -.
DR STRING; 391165.GbCGDNIH1_2392; -.
DR PRIDE; Q0BPG2; -.
DR EnsemblBacteria; ABI63290; ABI63290; GbCGDNIH1_2392.
DR GeneID; 56916772; -.
DR KEGG; gbe:GbCGDNIH1_2392; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001963; 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..915
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008249"
FT DOMAIN 414..584
FT /note="tr-type G"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..295
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 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 61..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..295
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 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 915 AA; 98696 MW; FC7706E7F303457B CRC64;
MSEGNDQDAG KGRLSLRPAG RMELGRTVDA GSVRQSFSHG RSKVVQVEVR KKRGLQPGTP
SAPEGGSSSA PAPQSGNAPQ GTPRSGGGNR GSGRGGAGGA GRALTAQELA IRQRVLEQQR
VEAARREVER REQEKISILS AAEEARRREE EAKRAAEEEA RRKEQEEADR IAAEAARKAA
ESAPPAEAPP VPPPAQRERT AAPSSRSAPS RTAPSDDIRR PSRPAPIPSK VPVAAPSAPQ
TLRLRERGDE GEEERKPRRA GGGGAPAPRK AAAPVAKKAV AEPRRGGRID VRAAIEGEDE
RTRSIASMRR QRDRERRQAE LERLRADQLK VVRDVVLPET IAVGELANRM AVRAADVIKQ
LMRMGMMATV TQTIDADTAE LVVQEFGHRV RRVSESDVEV GLEGISDIDS DLQPRPPVVT
VMGHVDHGKT SLLDALRATD VAAGEAGGIT QHIGAYQVTL PSRQKLTFLD TPGHEAFTAM
RSRGASVTDI VVLVVAADDG VMPQTIEAIK HAKAANAPII VAINKCDKPG ANPGRVRQEL
LHHEIVVEDM GGDTQDVEVS ALKRQNLDKL EEAILLQAEV LDLKANPDRA AEGTVVESRL
DRGRGPVATV LVQKGTLRQG DIVVAGAEWG RVRAMLDDKG QQMKEALPST PVEILGLAGV
PSAGEPFVAV ENESRAREIS EFRQRKIREK MAAGIAAGRG TLEQMLSRIQ AGAQKEVAVV
IKADVQGSAE AIATTVQKQE HEEVKVRTLL SSVGQISESD VQLAKASNAV LIAFNVRATN
QARELAQREG VDIRYYSIIY EVADDIEALV RGKIAPKQRE KFLGYAEIRK VFEITKVGKV
AGCMVTEGVV KRGCGVRLLR DNVVIHTGEL SQLKRFKDDV KEVARNYECG LSFAGYNDIK
EGDVVECYET ELVPA
