IF2_HAMD5
ID IF2_HAMD5 Reviewed; 882 AA.
AC C4K3F0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=HDEF_0331;
OS Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; aphid secondary symbionts; Candidatus Hamiltonella.
OX NCBI_TaxID=572265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5AT;
RX PubMed=19451630; DOI=10.1073/pnas.0900194106;
RA Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.;
RT "Hamiltonella defensa, genome evolution of protective bacterial
RT endosymbiont from pathogenic ancestors.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(2009).
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; CP001277; ACQ67093.1; -; Genomic_DNA.
DR RefSeq; WP_012738054.1; NC_012751.1.
DR AlphaFoldDB; C4K3F0; -.
DR SMR; C4K3F0; -.
DR STRING; 572265.HDEF_0331; -.
DR PRIDE; C4K3F0; -.
DR EnsemblBacteria; ACQ67093; ACQ67093; HDEF_0331.
DR GeneID; 66260246; -.
DR KEGG; hde:HDEF_0331; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000002334; 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; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF46955; SSF46955; 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; Reference proteome.
FT CHAIN 1..882
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000202777"
FT DOMAIN 382..551
FT /note="tr-type G"
FT REGION 95..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..398
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 416..420
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 437..440
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 491..494
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 527..529
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 112..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 391..398
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 437..441
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 491..494
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 882 AA; 97372 MW; 5111018697379287 CRC64;
MTDVTVKSLA EEIKTSVDRL VQQFFDAGIK KSQTDTVTQQ EKEKLLAHLN RQQGTVDNQL
TLQRKTRSVL NIQVTGGKSK TVHIEVRKKR TYVNPSVTKP EAPLPEEENA QIPKITKNTF
SQESLNKTSP QKSLKTKAIE KAKIESPKKE RHSLKEKQKK EAQSEKARRE AEASSLKRFA
EEEVRRKVEE EAKRVAEQAR KMAIENEAKW SELVADQIDS VDYHVTTSEH ARAAEDENDA
KVEGDRRSRH RGTKTTKQKK TNKLSESKTD REEARAVVRK SKRKPSALQQ SFNKPVVALN
RDVVIGETIS VAELANKMAV KGSQVIKAMM KLGAMATINQ VIDQETAQLV AEEMGHKVIL
RRENELEEAL MSDRDTGVLT VHRAPVVTIM GHVDHGKTSL LDYIRSTKVA TGEAGGITQH
IGAYHVETEN GMITFLDTPG HAAFTSMRAR GAQATDIVVL VVAADDGVMP QTIEAIQHAK
AAKVPVVVAV NKIDKAEADP DRVKKELIQH GIQPEEWGGD SQFIHVSAKV GTGIDDLLNA
ILLQAEVLEL KAVKSGMANG VVIESFLDKG RGPVATVLVQ EGTLNKGDIV LCGFQYGRVR
AMRNELGREV ISAGPSIPVE ILGLSSVSSA GDAVTVVRDE KKAREVALYR QGKFREIKLA
RQQKSKLENM FDSLREGEIS ELNIVLKSDV QGSCEAIREA LQKLSTDEVK IKIIGSGVGG
ITETDATLAA ASNAIILGFN VRADAATRRL VEAENLNLRY YSVIYDLLDE VKQAMSGMLS
PKYEQKIIGL AEVRDVFKSP KFGAIAGCMV VEGLIKRSSP IRVLRNNVVI YEGELESLRR
FKDDVNEVRN GIECGIGVKN YDVQVNDTIE VFEIIEIKRT IS
