IF2_RALSO
ID IF2_RALSO Reviewed; 964 AA.
AC Q8XZV6;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=RSc1289;
GN ORFNames=RS02965;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
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; AL646052; CAD14991.1; -; Genomic_DNA.
DR RefSeq; WP_011001238.1; NC_003295.1.
DR AlphaFoldDB; Q8XZV6; -.
DR SMR; Q8XZV6; -.
DR STRING; 267608.RSc1289; -.
DR EnsemblBacteria; CAD14991; CAD14991; RSc1289.
DR GeneID; 60500810; -.
DR KEGG; rso:RSc1289; -.
DR PATRIC; fig|267608.8.peg.1311; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001436; 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..964
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137239"
FT DOMAIN 464..633
FT /note="tr-type G"
FT REGION 150..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..480
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 498..502
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 519..522
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 573..576
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 609..611
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 150..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 473..480
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 519..523
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 573..576
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 964 AA; 103313 MW; 6BAB22BEE2DDD913 CRC64;
MASTTVAQLA GELNRSAAAL LEQLQAAGVQ KATPEDVITE SDKTRLLDYL KRAHGSAEDG
ARKKITLTKR ETSEIRQADA TGKTRTVQVE VRKKRVLMKR DEAGAAPAEA EAPAPVTAPV
VDVEEVARRE EEQRRQAELL ARQEAELKAR QEAMEREEAE RRARQEAAEA EQRRQAELAA
KKAEEEAAAA RAAAEASDEA PRRKAEEDAA RLASEREAAQ KAAEEARAAA DKIKAEEDGA
RKRREAAEAE ARAIREMMNA PARVLKTPAE RKAEEKKAEQ SGTLHKPVKA AGEARPAPAA
KKAAAPAAAP AATPAGDKKG GRGGKPGGWQ DDARGNKRGG LKTRGDTGGG VDGWRGSKGG
RNRHGDDNRN AFQAPTEPVV REVHVPETIS VAELAHKMAV KAAEVIKQMM KLGQMVTINQ
VLDQETAMIV VEEMGHQAVA AKLDDPEALL VEGVQEQQNV EAEARPPVVT VMGHVDHGKT
SLLDYIRRAK VAAGEAGGIT QHIGAYHVET PRGVITFLDT PGHEAFTAMR ARGAKATDIV
ILVVAADDGV MPQTKEAIAH AKAAGVPIVV AINKIDKPEA NPDRVKQELV SESVIPEEYG
GDSPFVPVSA KTGQGIENLL ENVLLQAEVL ELKAPINAAA KGLVVEAQLD KGKGPIATVL
VQSGTLKRGD VVLAGTAYGR VRAMLDENGK PAKEAGPSIP VEIQGLSEVP GAGEEVIVLP
DERKAREIAL FRQGKFRDVK LARQQAAKLE TMLEQMSEGE VKTLPLIIKA DVQGSQEALV
HALNKLSTGE VRVQVVHGAV GGISESDVNL ATASKAVIIG FNTRADAGAR KLAEHQGIDI
RYYNIIYDAV DEVKAAMSGM LSPEKKEETT GLVEVRQVFH VPKVGAVAGC MVLDGVVKRS
SLVRVLRENV VIFSGELESL KRFKDDVKEV KQGFECGLSI KNFNDVKEGD QLEIYEITEV
ARTL
