IF2_HAEIG
ID IF2_HAEIG Reviewed; 844 AA.
AC A5UF34;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=CGSHiGG_01560;
OS Haemophilus influenzae (strain PittGG).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=374931;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PittGG;
RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA Ehrlich G.D.;
RT "Characterization and modeling of the Haemophilus influenzae core and
RT supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT nontypeable strains.";
RL Genome Biol. 8:R103.1-R103.18(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; CP000672; ABQ99389.1; -; Genomic_DNA.
DR AlphaFoldDB; A5UF34; -.
DR SMR; A5UF34; -.
DR EnsemblBacteria; ABQ99389; ABQ99389; CGSHiGG_01560.
DR KEGG; hiq:CGSHiGG_01560; -.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001990; 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..844
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008250"
FT DOMAIN 343..513
FT /note="tr-type G"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..359
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 377..381
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 399..402
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 453..456
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 489..491
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 352..359
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 399..403
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 453..456
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 844 AA; 92152 MW; BCAF4BD33D9951FE CRC64;
MTEDVKADVP KKLSIQRRTK TTVSGTTTSG KSKAVQVEVR KKRTVKTDIA QQEEAKLKAQ
QEAEAKKIAE QKAAEEKARL EAEKAATKKE ADEKSKAEKA KAETAKPAKS AVDSKAKFVD
PEKEKRKAEE AELRRKAEEV ARQKAEEQAR RAAEEAKRYA EADDSDNESS SEDYSDYNLS
SRYALEAEDE EDRRNENRGR GKNKVAKAKK GGRDDENSKN SKNERESNRK NQKDAKFGKG
KNGKKGAALQ QAFTKPAQVV KSDVVIGETI TVAELANKMA VKATEIIKMM MKMGEMVTIN
QVIDQETAQL VAEELGHKVI LRNENELEEA VLGDRDVNAE KVTRAPVVTI MGHVDHGKTS
LLDYIRKAKV AAGEAGGITQ HIGAYHVEMD DGKMITFLDT PGHAAFTSMR ARGAKATDIV
VLVVAADDGV MPQTIEAIQH AKAAGAPLVV AVNKIDKPEA NPDRVEQELL QHDVISEKFG
GDVQFVPVSA KKGTGVDDLL DAILLQSEVL ELTAVKDGMA SGVVIESYLD KGRGPVATIL
VQSGTLRKGD IVLCGFEYGR ARAMRDENGK EVDEAGPSIP VELLGLSGVP AAGDEATVVR
DEKKAREVAL YRQGKFREVK LARQQKAKLE NMFSNMSEGD VAELNVIVKA DVQGSVEAIV
QALNELSTNE VKVKVVGSGV GGITETDATL ATASNAIIVG FNVRADATAR RVIEAENIDL
RYYSIIYELL NEIKAAMSGM LEPEFKQEII GLAEVRDVFR HPKFGAIAGC MVTEGVVKRN
NPIRVLRDNV VIFEGELESL RRFKDDVSEV RNGMECGIGV KNYNDVKVGD QIEVFEVVEV
KRSI
