IF2_HELPG
ID IF2_HELPG Reviewed; 937 AA.
AC B5Z6E6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=HPG27_380;
OS Helicobacter pylori (strain G27).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=563041;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G27;
RX PubMed=18952803; DOI=10.1128/jb.01416-08;
RA Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S.,
RA Ottemann K.M., Stein M., Salama N.R., Guillemin K.;
RT "The complete genome sequence of Helicobacter pylori strain G27.";
RL J. Bacteriol. 191:447-448(2009).
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; CP001173; ACI27145.1; -; Genomic_DNA.
DR RefSeq; WP_001293376.1; NC_011333.1.
DR AlphaFoldDB; B5Z6E6; -.
DR SMR; B5Z6E6; -.
DR EnsemblBacteria; ACI27145; ACI27145; HPG27_380.
DR KEGG; hpg:HPG27_380; -.
DR HOGENOM; CLU_006301_4_0_7; -.
DR OMA; VIFAMNK; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001735; 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; 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..937
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093792"
FT DOMAIN 436..605
FT /note="tr-type G"
FT REGION 61..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..452
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 470..474
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 491..494
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 545..548
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 581..583
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 91..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 445..452
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 491..495
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 545..548
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 937 AA; 104641 MW; 3EEABFAF9C52833C CRC64;
MSEMVDLKEF LAELGKTQKE LKNVIEQAKD IGLELKTNSK MTPEEANKLY KYIVEGIKEQ
IQANQPAKNP EQDNKDDLNT AVASKPLNKK VSKTPKKEEK SQPKPKKTKE KKKEAPTPIA
KKKGGIEIVN TFENQTPPVE NNPKVVSHSQ IEKAKQKLQE IQKSREALNK LTQSNANNAK
KEISEVKKQE QEIKRHENIK RRTGFRVIKR NDEVENESEN SVTESKKPTQ SAAAIFEDIK
KEWQEKDKQE AKKAKKPSKP KATPTAKNNK SHKIDFSDAR DFKGNDIYDD ETDEILLFDL
HEQDNFNKEE EEKEIRQNIN DRVRVQRKNP WMNESGIKRQ SKKKRAFRND NSQKVIQSAI
AIPEEVRVYE FAQKANLNLA DVIKTLFNLG LMVTKNDFLD KDSIEILAEE FHLEISVQNT
LEEFEVEEVL EGVKKERPPV VTIMGHVDHG KTSLLDKIRD KRVAHTEAGG ITQHIGAYMV
EKNGKWVSFI DTPGHEAFSQ MRNRGAQVTD IAVIVIAADD GVKQQTIEAL EHAKAANVPV
IFAMNKMDKP NVNPDKLKAE CAELGYNPVD WGGEHEFIPV SAKTGDGIDN LLETILIQAD
IMELKAIEEG SARAVVLEGS VEKGRGAVAT VIVQSGTLSV GDSFFAETAF GKVRTMTDDQ
GKSIQNLKPS MVALITGLSE VPPAGSVLIG VENDSIARLQ AQKRATYLRQ KALSKSTKVS
FDELSEMVAN KELKNIPVVI KADTQGSLEA IKNSLLELNN EEVAIQVIHS GVGGITENDL
SLVSSSDHAV ILGFNIRPTG NVKNKAKEYN VSIKTYTVIY ALIEEMRSLL LGLMSPIIEE
EHTGQAEVRE TFNIPKVGTI AGCVVSDGVI ARGIKARLIR DGVVVHTGEI LSLKRFKDDV
KEVSKGYECG IMLDNYNEIK VGDVFETYKE IHKKRTL
