IF2_HELPJ
ID IF2_HELPJ Reviewed; 949 AA.
AC Q9ZM46;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB; OrderedLocusNames=jhp_0377;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
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; AE001439; AAD05948.1; -; Genomic_DNA.
DR PIR; E71940; E71940.
DR RefSeq; WP_001282226.1; NC_000921.1.
DR AlphaFoldDB; Q9ZM46; -.
DR SMR; Q9ZM46; -.
DR STRING; 85963.jhp_0377; -.
DR PRIDE; Q9ZM46; -.
DR EnsemblBacteria; AAD05948; AAD05948; jhp_0377.
DR KEGG; hpj:jhp_0377; -.
DR eggNOG; COG0532; Bacteria.
DR OMA; VIFAMNK; -.
DR Proteomes; UP000000804; 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..949
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137210"
FT DOMAIN 448..617
FT /note="tr-type G"
FT REGION 61..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..464
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 482..486
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 503..506
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 557..560
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 593..595
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 91..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 457..464
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 503..507
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 557..560
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 949 AA; 105962 MW; FA8969B0C64B3278 CRC64;
MSDMVDLKKF VTELGKTQKE LKNVIEQAKD IGLELKTNFK MTPEQAGKLY KYIVDGIKEQ
IQANQPTKNP KQDNKDDLNT AATPKPLAKK ASKTPKKEET KAQPKPKKTK EKKKEAPAPI
IKKKEIEIVN TFENQTPLVE NTPKAVSHSQ IEKAKQKLQE IQKSREALNK LTQSNTNTTN
NANSASNVSN AKKEISEVKK QEQEIKRHEN IKRRTGFRVI KRNDETENET ENSVTESKKP
TQSAAAIFED IKKEWQEKDK QETKKTKKPS KPKATPTAKN NKSHKIDFSD VRDFKGNDIY
DDETDEILLF DLHEQDNLNK EEEEKEARQN INDRVRVQRK NPWMNEAGIK RQSKKKRVFR
NDNSQKVIQS AIAIPEEVRV YEFAQKANLN LADVIKTLFN LGLMVTKNDF LDKDSIEILA
EEFHLEISVQ NTLEEFEVEE VLEGVKKERP PVVTIMGHVD HGKTSLLDKI RDKRVAHTEA
GGITQHIGAY MVEKNNKWVS FIDTPGHEAF SQMRNRGAQV TDIAVIVIAA DDGVKQQTIE
ALEHAKAANV PVIFAMNKMD KPNVNPDKLK AECAELGYNP VDWGGEHEFI PVSAKTGDGI
DNLLETILIQ ADIMELKAIE EGSARAVVLE GSVEKGRGAV ATVIVQSGTL SVGDSFFAET
AFGKVRTMTD DQGKSIQNLK PSMVALITGL SEVPPAGSVL IGVENDSIAR LQAQKRATYL
RQKALSKSTK VSFDELSEMV ANKELKNIPV IIKADTQGSL EAIKNSLLEL NNEEVAIQVI
HSGVGGITEN DLSLVSSSEH AVILGFNIRP TGNVKNKAKE YNVSIKTYTV IYALIEGMRS
LLLGLMSPII EEEHTGQAEV RETFNIPKVG TIAGCVVSDG EIARGIKARL IRDGVVVHTG
EILSLKRFKD DVKEVSKGYE CGIMLDNYNE IKVGDVFETY KEIHKKRTL
