ID IF2_HELPY Reviewed; 944 AA.
AC P55972;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 27-MAR-2024, entry version 145.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB; OrderedLocusNames=HP_1048;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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}.
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DR EMBL; AE000511; AAD08093.1; -; Genomic_DNA.
DR PIR; H64650; H64650.
DR RefSeq; NP_207839.1; NC_000915.1.
DR RefSeq; WP_000016275.1; NC_018939.1.
DR AlphaFoldDB; P55972; -.
DR SMR; P55972; -.
DR DIP; DIP-3291N; -.
DR IntAct; P55972; 5.
DR MINT; P55972; -.
DR STRING; 85962.HP_1048; -.
DR PaxDb; 85962-C694_05420; -.
DR EnsemblBacteria; AAD08093; AAD08093; HP_1048.
DR KEGG; hpy:HP_1048; -.
DR PATRIC; fig|85962.47.peg.1127; -.
DR eggNOG; COG0532; Bacteria.
DR InParanoid; P55972; -.
DR OrthoDB; 9811804at2; -.
DR PhylomeDB; P55972; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 1.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
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; Reference proteome.
FT CHAIN 1..944
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137209"
FT DOMAIN 443..612
FT /note="tr-type G"
FT REGION 61..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..459
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 477..481
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 498..501
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 552..555
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 588..590
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 130..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 452..459
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 498..502
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 552..555
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 944 AA; 105195 MW; EC90404D9C3B851D CRC64;
MSGMVDLKEF LAELGKTQKE LKNVIEQAKD IGLELKTNSK MTPEQAGKLY KYIVDGIKEQ
IQANQPAKNP EQDNKDDLNT AVASKSLNKK VSKTPKKEET KSQPKPKKTK EKKKEAPTPI
AKKKGGIEIV NTFENQTPPT ENTPKVVSHS QIEKAKQKLQ EIQKSREALN KLTQSNANNA
SNANNAKKEI SEVKKQEQEI KRHENIKRRT GFRVIKRNDE VENESENSVT ESKKPTQSAA
AIFEDIKKEW QEKDKQEAKK AKKPSKPKAT PTAKNNKSHK IDFSDARDFK GNDIYDDETD
EILLFDLHEQ DNFNKEEEEK EIRQNINDRV RVQRKNPWMN ESGIKRQSKK KRAFRNDNSQ
KVIQSTTAIP EEVRVYEFAQ KANLNLADVI KTLFNLGLMV TKNDFLDKDS IEILAEEFHL
EISVQNTLEE FEVEEVLEGV KKERPPVVTI MGHVDHGKTS LLDKIRDKRV AHTEAGGITQ
HIGAYMVEKN DKWVSFIDTP GHEAFSQMRN RGAQVTDIAV IVIAADDGVK QQTIEALEHA
KAANVPVIFA MNKMDKPNVN PDKLKAECAE LGYNPVDWGG EHEFIPVSAK TGDGIDNLLE
TILIQAGIME LKAIEEGSAR AVVLEGSVEK GRGAVATVIV QSGTLSVGDS FFAETAFGKV
RTMTDDQGKS IQNLKPSMVA LITGLSEVPP AGSVLIGVEN DSIARLQAQK RATYLRQKAL
SKSTKVSFDE LSEMVANKEL KNIPVVIKAD TQGSLEAIKN SLLELNNEEV AIQVIHSGVG
GITENDLSLV SSSEHAVILG FNIRPTGNVK NKAKEYNVSI KTYTVIYALI EEMRSLLLGL
MSPIIEEEHT GQAEVRETFN IPKVGTIAGC VVSDGVIARG IKARLIRDGV VIHTGEILSL
KRFKDDVKEV SKGYECGIML DNYNEIKVGD VFETYKEIHK KRTL
//
