IF2_HELP2
ID IF2_HELP2 Reviewed; 947 AA.
AC B6JKX5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=HPP12_0396;
OS Helicobacter pylori (strain P12).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=570508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P12;
RA Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.;
RT "The complete genome sequence of Helicobacter pylori strain P12.";
RL Submitted (OCT-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; CP001217; ACJ07553.1; -; Genomic_DNA.
DR RefSeq; WP_001293382.1; NC_011498.1.
DR AlphaFoldDB; B6JKX5; -.
DR SMR; B6JKX5; -.
DR EnsemblBacteria; ACJ07553; ACJ07553; HPP12_0396.
DR KEGG; hpp:HPP12_0396; -.
DR HOGENOM; CLU_006301_4_0_7; -.
DR OMA; VIFAMNK; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000008198; 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..947
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093791"
FT DOMAIN 446..615
FT /note="tr-type G"
FT REGION 61..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..462
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 480..484
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 501..504
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 555..558
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 591..593
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 91..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 455..462
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 501..505
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 555..558
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 947 AA; 105682 MW; FE2C4C36621F1DC4 CRC64;
MSEMVDLKEF LAELGKTQKE LKNVIEQAKD IGLELKTNSK MTPEQAGKLY KYIVDGIKEQ
IQANQPAKNP EQDNKDDLNT AVASKSLNKK VFKTPKKEET KSQPKPKKTK EKKKEAPTPI
AKKKGGIEIV NTFEDQTPPV ENAPKVVSHS QIEKAKQKLQ EIQKSREALN KLTQSNANNA
NSTNNANNAK KEISEVKKQE QEIKRHENIK RRTGFRVIKR NDETENETEN SVTESKKPTQ
SAAAIFEDIK KEWQEKDKQE AKKVKKPSKP KATPTAKNNK SHKIDFSDAR DFKGNDIYDD
ETDEILLFDL HEQDNLNKEE EEKEIRQNIN DRVRVQRKNP WMNESGIKRQ SKKKRAFRND
NSQKVIQSAI AIPEEVRVYE FAQKANLNLA DVIKTLFNLG LMVTKNDFLD KDSIEILAEE
FHLEISVQNT LEEFEVEEVL EGVKKERPPV VTIMGHVDHG KTSLLDKIRD KRVAHTEAGG
ITQHIGAYMV EKNNKWVSFI DTPGHEAFSQ MRNRGAQVTD IAVIVIAADD GVKQQTIEAL
EHAKAANVPV IFAMNKMDKP NVNPDKLKAE CAELGYNPVD WGGEHEFIPV SAKTGDGIDN
LLETILIQAD IMELKAIEEG SARAVVLEGS VEKGRGAVAT VIVQSGTLSV GDSFFAETAF
GKVRTMTDDQ GKSIQNLKPS MVALITGLSE VPPAGSVLIG VENDSIARLQ AQKRATYLHQ
KALSKSTKVS FDELSEMVAN KELKNIPVVI KADTQGSLEA IKNSLLELNN EEVAIQVIHS
GVGGITENDL SLVSNSEHAV ILGFNIRPTG NVKNKAKEYN VSIKTYTVIY ALIEEMRSLL
LGLMSPIIEE EHTGQAEVRE TFNIPKVGTI AGCVVSDGVI ARGIKARLIR DGVVIHTGEI
LSLKRFKDDV KEVSKGYECG IMLDNYNEIK VGDVFETYKE IHKKRTL
