IF2_HAEI8
ID IF2_HAEI8 Reviewed; 844 AA.
AC Q4QK37;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=NTHI1844;
OS Haemophilus influenzae (strain 86-028NP).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=281310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=86-028NP;
RX PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA Munson R.S. Jr.;
RT "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL J. Bacteriol. 187:4627-4636(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000057; AAX88610.1; -; Genomic_DNA.
DR RefSeq; WP_011272663.1; NC_007146.2.
DR AlphaFoldDB; Q4QK37; -.
DR SMR; Q4QK37; -.
DR PRIDE; Q4QK37; -.
DR EnsemblBacteria; AAX88610; AAX88610; NTHI1844.
DR KEGG; hit:NTHI1844; -.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 106139at2; -.
DR Proteomes; UP000002525; 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_0000228203"
FT DOMAIN 343..513
FT /note="tr-type G"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..249
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..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Basic and acidic 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; 92208 MW; F8A8F4053C919D70 CRC64;
MTEDVKADAP KKLSIQRRTK TTVSSTTTGG KSKEVQVEVR KKRTVKTDIA QQEEAKLKAQ
QEAEAKKIAE QKAAEEKARL EAEKAATKKE ADEKSKAEKA KAETAKPAKS AVDSKAKFVD
PEKEKRKAEE AELRRKAEEV ARQKAEEQAR RAAEEAKRYA EADDSDNESS SEDYSDYNLS
SRYALEAEDE EDRRNENRGR GKNKVAKAKK GGRDDENSKN SKNERESNRK NQKDAKFGKG
KNGKKGTALQ QAFTKPVQVV KADVVIGETI TVAELANKMS VKATEIIKVM 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
