IF2_CUPPJ
ID IF2_CUPPJ Reviewed; 966 AA.
AC Q46ZP1;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Reut_A2028;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
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; CP000090; AAZ61392.1; -; Genomic_DNA.
DR RefSeq; WP_011298190.1; NC_007347.1.
DR AlphaFoldDB; Q46ZP1; -.
DR SMR; Q46ZP1; -.
DR STRING; 264198.Reut_A2028; -.
DR PRIDE; Q46ZP1; -.
DR EnsemblBacteria; AAZ61392; AAZ61392; Reut_A2028.
DR KEGG; reu:Reut_A2028; -.
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..966
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228234"
FT DOMAIN 466..635
FT /note="tr-type G"
FT REGION 99..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..482
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 500..504
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 521..524
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 575..578
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 611..613
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 120..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 475..482
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 521..525
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 575..578
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 966 AA; 103796 MW; 04CBEB7A776AD8F0 CRC64;
MASTTVAQLA AELSRSAAAL LEQLQAAGLG KATPEDIVTE SDKTRLLDYL KRSHGQADDS
ARKKITLTKR ETSEIRQADS TGKTRTVQVE VRKKRVLIKR DEAGADQHNE AADQHALAAE
AAEQARREEE ERQQAAELAR QEAEAKARRE AAEREEAERR AKQEALEAEQ RRQAELLARK
AEEEAAAARA VGEAAEDASR KKAEDEQARV AVERAAAQKA ADDAKAAADK ARAEQDAARK
RREAAEAEAR AIQQMLNAPA RVLKAPSERK AEEKKAEQTG TLHKPVKPAS ATATEAKAGD
KKPAATTTTT TATTTADKKG KTGKPGSWQD DSSRKKGSGL KTRGDSSGGV GGWRGGPRGR
GGRQQHADDG RSNFQAPTEP VVREVHVPET ISVADLAHKM AVKASEVIKQ MMKLGQMVTI
NQVLDQETAM IVVEEMGHKA FAAKLDDPEA LLVVDGEEHT DAEQLPRPPV VTVMGHVDHG
KTSLLDYIRR AKVAAGEAGG ITQHIGAYHV ETERGVITFL DTPGHEAFTA MRARGAKATD
IVILVVAADD GVMPQTKEAI AHAKAAGVPI VVAINKIDKP DANPDRVKQE LVAEQVLPEE
YGGDSPFVPV SAKTGAGIED LLEQVLLQAE VLELKAPVDA PAKGLVVEAQ LDKGKGPIAT
ILVSSGTLKR GDVVLAGSAY GRVRAMLDEN GKPTKEAGPS IPVEIQGLSE VPAAGEEVLV
LPDERKAREI ALFRQGKFRD VKLAKQQAAK LETMLEQMTE GDVQTLPLIV KADVQGSQEA
LVQSLQKLST AEVRVQIVHA GVGAISESDV NLATASKAVI IGFNVRADAG ARKLAENHGI
DIRYYNIIYD AVDEIKAAMS GMLAPEKRET TIGQVEVRQV FRVPKIGAVA GCMVTDGLVK
RNSLVRVLRN NVVVHTGELD SLKRFKDDVK EVKQGFECGL SIKNFNDVQE GDQLEVYEIT
EVARTL
