IF2_SULNB
ID IF2_SULNB Reviewed; 906 AA.
AC A6QBQ5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SUN_1971;
OS Sulfurovum sp. (strain NBC37-1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Sulfurovaceae; Sulfurovum; unclassified Sulfurovum.
OX NCBI_TaxID=387093;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBC37-1;
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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; AP009179; BAF72914.1; -; Genomic_DNA.
DR RefSeq; WP_012083734.1; NC_009663.1.
DR AlphaFoldDB; A6QBQ5; -.
DR SMR; A6QBQ5; -.
DR STRING; 387093.SUN_1971; -.
DR EnsemblBacteria; BAF72914; BAF72914; SUN_1971.
DR KEGG; sun:SUN_1971; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_4_1_7; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000006378; 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; 2.
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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..906
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008358"
FT DOMAIN 405..574
FT /note="tr-type G"
FT REGION 94..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..421
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 439..443
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 460..463
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 514..517
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 550..552
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 165..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 414..421
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 460..464
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 514..517
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 906 AA; 98543 MW; 6ED9B6728D294EB6 CRC64;
MDKVKIQEIA EEAGLSNGEL IEKAKELGFN VKAANSAISM DDAGILVDFA ISGTLPKGFK
KPGEKPKLKV VKKKTVEKEP ETIVEAPVIE KETAPEKTEV IPEETENTVE ESTAAETVES
EPETAVIEEI ETPAETAKEE TVEAAPVVKE VKQRKGISVV SKKAESEAEK GTEIEKPKRR
TLSRTGIKIV RKAKPAPVRA ATRISMGSGA PTPPSKKKVK KGPAEARETG KKIDIFNHDS
MSGDIDSGFG EEEVVLLDFS DKNIYEDMMR QEQKRREEAK KREAANGGPA KGRQPFRPQQ
RRSLKRGGKR KKYTKEESSE VITSVEIPEN VRVYEFAEKV NRSVGEVVKV LFALGMMVTK
NDFLSKDEIE ILAEEFGVEV STMNPLDELD YVQAYDEVED THLEERPPVI TIMGHVDHGK
TSLLDKIRSA KVADKEAGGI TQHVGAYQVE KNGKKITFVD TPGHEAFTEM RARGAQATDI
VIIVVAADDG VMPQTKEAIA HTKAAGVPMI IAMNKMDKES ANPDNIKSQL AEIDVMAADW
GGEYEFVPVS AHTGLGIDDL LETILLQAEM MELKADPTRK AKAVVVESSV EKGFGPVANV
IIKNGTLHVG DNVIVGTTYG RIKAIKLDDG SAVKEIGPST PAAIVGLNEV PGAGEALVAM
DTDKEVRELA EKRAEYDRAK QLSKSTKASL DDLSALIAEG QLKSLPVIIK ADVQGSLEAI
KGSLEKLRNE EVKVNIIHEG VGGVTESDVT LADASEHAVI LGFNVRPTGS VKKKAKELGV
EVRTYTIIYD LLDDVKALLG GMMSPVIKEE VTGQAEVRET FVVGKVGTIA GCKVSDGVIT
RNSKARLIRD GVVVYESKIS SLKRFNEDAR EVKNGYECGI MLENFNDIKE GDVIETFKDV
EEQVTL
