IF2_HELPH
ID IF2_HELPH Reviewed; 944 AA.
AC Q1CUA6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=HPAG1_0399;
OS Helicobacter pylori (strain HPAG1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=357544;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPAG1;
RX PubMed=16788065; DOI=10.1073/pnas.0603784103;
RA Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A.,
RA Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G.,
RA Gordon J.I.;
RT "The complete genome sequence of a chronic atrophic gastritis Helicobacter
RT pylori strain: evolution during disease progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006).
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; CP000241; ABF84466.1; -; Genomic_DNA.
DR RefSeq; WP_000016270.1; NC_008086.1.
DR AlphaFoldDB; Q1CUA6; -.
DR SMR; Q1CUA6; -.
DR PRIDE; Q1CUA6; -.
DR EnsemblBacteria; ABF84466; ABF84466; HPAG1_0399.
DR KEGG; hpa:HPAG1_0399; -.
DR HOGENOM; CLU_006301_4_0_7; -.
DR OMA; VIFAMNK; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000008835; 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..944
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008253"
FT DOMAIN 443..612
FT /note="tr-type G"
FT REGION 61..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 151..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..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:0000255|HAMAP-Rule:MF_00100"
FT BINDING 498..502
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 552..555
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 944 AA; 105400 MW; CF96F519DEE01C3E CRC64;
MSGMVDLKEF LAELGKTQKE LKNVIEQAKD IGLELKTNSK MTPEQAGKLY KYIVDGIKEQ
IQANQPAKNP EQDNKDDLNM VQTPKPLNKK VSKTPKKEET KSQPKPKKTK EKKKEAPTPI
AKKKGGIEIV NTFENQTPPT ENTPKVVSHS QIEKAKQKLQ EIQKSREALN KLTQSNANNA
SNTNNAKKEI SEVKKQEQEI KRHENIKRRT GFRVIKRNDE TENESENSVT ESKKPTQSVA
AIFEDIKKEW QEKDKQEAKK AKKPSKPKAT PTAKNNKSHK IDFSDARDFK GNDIYDDETD
EILLFDLHEQ DNLNKEEEEK EIRQNINDRV RVQRKNPWMN ESGIKRQSKK KRAFRNDNSQ
KVIQSTIAIP EEVRVYEFAQ KANLNLADVI KTLFNLGLMV TKNDFLDKDS IEILAEEFHL
EISVQNTLEE FEVEEVLEGV KKERPPVVTI MGHVDHGKTS LLDKIRDKRV AHTEAGGITQ
HIGAYMVEKN DKWVSFIDTP GHEAFSQMRN RGAQVTDIAV IVIAADDGVK QQTIEALEHA
KAANVPVIFA MNKMDKPNVN PDKLKAECAE LGYNPVDWGG EHEFIPVSAK TGDGIDNLLE
TILIQADIME LKAIEEGSAR AVVLEGSVEK GRGAVATVIV QSGTLSVGDS FFAETAFGKV
RTMTDDQGKS IQNLKPSMVA LITGLSEVPP AGSVLIGVEN DSIARLQAQK RATYLRQKAL
SKSTKVSFDE LSEMVANKEL KNIPVVIKAD TQGSLEAIKN SLLELNNEEV AIQVIHSGVG
GITENDLSLV SSSDHAVILG FNIRPTGNVK NKAKEYNVSI KTYTVIYALI EEMRSLLLGL
MSPIIEEEHT GQAEVRETFN IPKVGTIAGC VVSDGVIARG IKARLIRDGV VVHTGEILSL
KRFKDDVKEV SKGYECGIML DNYNEIKVGD VFETYKEIHK KRTL
