IF2_RALPJ
ID IF2_RALPJ Reviewed; 964 AA.
AC B2UAA3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Rpic_1117;
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12J;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT "Complete sequence of chromosome 1 of Ralstonia pickettii 12J.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001068; ACD26265.1; -; Genomic_DNA.
DR RefSeq; WP_012435351.1; NC_010682.1.
DR AlphaFoldDB; B2UAA3; -.
DR SMR; B2UAA3; -.
DR STRING; 402626.Rpic_1117; -.
DR PRIDE; B2UAA3; -.
DR EnsemblBacteria; ACD26265; ACD26265; Rpic_1117.
DR KEGG; rpi:Rpic_1117; -.
DR PATRIC; fig|402626.5.peg.2323; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
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.
FT CHAIN 1..964
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093816"
FT DOMAIN 464..633
FT /note="tr-type G"
FT REGION 105..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..378
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 146..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..340
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; 103458 MW; 051CF60030368121 CRC64;
MASTTVAQLA GELNRSASAL LEQLQAAGVQ KATPEDVITE SDKTRLLDYL KRAHGSAEDG
ARKKITITKR ETSEIRQADA TGKTRTVQVE VKKKRVLVKR DEPNAALAES EASEAAPVVD
AEEVARREEE HRRQAELLAR QEAELKARQE AMEREEAERR ARQEAAEAEQ KRQAELAAKK
AEEEAVAARA AAEASDEAPR RKAEEDAARL ATEREAAQKA ADEARVAADK IKAEEDAARK
RREAAEAEAR AIREMMSAPA RVLKTPAERK AEEVKKAEQS GTLHKPVKPA GEARPAAAKK
PAAPAPAAAP APGSPAGDKK GGRGKSGWQD DNRGGKRGGL KTRGDTGGGA DGWRSGSKGG
RNRHGDDNRN AFQAPTEPVV REVHVPETIS VADLAHKMSV KAAEVIKQMM KLGQMVTINQ
VLDQETAMIV VEEMGHQAVA AKLDDPEAML VGDVQEQTNA EAETRPPVVT VMGHVDHGKT
SLLDYIRRAK VAAGEAGGIT QHIGAYHVET DRGVITFLDT PGHEAFTAMR ARGAKATDIV
ILVVAADDGV MPQTKEAIAH AKAAGVPIVV AITKVDKPEA NPDRVKQELV AESVIPEEYG
GDVPFVPVSA KTGEGIDSLL ENVLLQAEVL ELKAPVNAPA KGLVVEAQLD KGKGPIATVL
VQSGTLKRGD VVLAGTAYGR VRAMLDENGK PAKDAGPSIP VEIQGLSEVP GAGEEVLVLP
DERKAREIAL FRQGKFRDVK LARQQAAKLE NMLEQMSEGD VKSLPLIIKA DVQGSQEALV
HSLKKLSTDE VRVQIVHAAV GGITESDVNL ATASKAVIIG FNTRADAGAR KLAENHGIDI
RYYNIIYDAV DEVKAAMSGM LSPEKREETT GLVEVRQVFH VPKVGAVAGC MVLDGFVKRN
SLVRVLRANV VIFSGELDSL KRFKDDVKEV KQGFECGLSI KNFNDVQEGD QLEVYEITEV
ARTL
