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
//