IF2_SALAR
ID IF2_SALAR Reviewed; 893 AA.
AC A9MP36;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SARI_04338;
OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=41514;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000880; ABX24118.1; -; Genomic_DNA.
DR RefSeq; WP_000133074.1; NC_010067.1.
DR AlphaFoldDB; A9MP36; -.
DR SMR; A9MP36; -.
DR STRING; 41514.SARI_04338; -.
DR EnsemblBacteria; ABX24118; ABX24118; SARI_04338.
DR KEGG; ses:SARI_04338; -.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002084; 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..893
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000075616"
FT DOMAIN 392..561
FT /note="tr-type G"
FT REGION 49..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..408
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 426..430
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 447..450
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 501..504
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 537..539
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 61..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 401..408
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 447..451
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 501..504
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 893 AA; 97417 MW; 4BDC1E595C47BE1B CRC64;
MTDVTVKALA AERQVSVDRL VQQFADAGIR KSADDSVSAQ EKQTLLAHLN REAGSGPDKL
TLQRKTRSTL NIPGTGGKSK SVQIEVRKKR TFVKRDPQEA ERLAAEEQAQ REAEEQARRE
AEEQAKREAQ QKAEREAAEQ AKREAAEKAK REAAEKDKVS NQQTDDMTKT AQAEKARREN
EAAELKRKAE EEARRKLEEE ARRVAEEARR MAEENKWTAT PEPVEDTSDY HVTTSQHARQ
AEDESDREVE GGRGRGRNAK AARPAKKGNK HAESKADREE ARAAVRGGKG GKRKGSSLQQ
GFQKPVQAVN RDVVIGETIT VGELANKMAV KGSQVIKAMM KLGAMATINQ VIDQETAQLV
AEEMGHKVIL RRENELEEAV MSDRDTGAAA EPRAPVVTIM GHVDHGKTSL LDYIRSTKVA
SGEAGGITQH IGAYHVETDN GMITFLDTPG HAAFTSMRAR GAQATDIVVL VVAADDGVMP
QTIEAIQHAK AAGVPVVVAV NKIDKPEADP DRVKNELSQY GILPEEWGGE SQFVHVSAKA
GTGIDELLDA ILLQAEVLEL KAVRKGMASG AVIESFLDKG RGPVATVLVR EGTLHKGDIV
LCGFEYGRVR AMRNELGQEV LEAGPSIPVE ILGLSGVPAA GDEVTVVRDE KKAREVALYR
QGKFREVKLA RQQKSKLENM FANMTEGEVH EVNIVLKADV QGSVEAISDS LLKLSTDEVK
VKIIGSGVGG ITETDATLAA ASNAILVGFN VRADASARKV IESESLDLRY YSVIYNLIDE
VKAAMSGMLS PELKQQIIGL AEVRDVFKSP KFGAIAGCMV TEGVVKRHNP IRVLRDNVVI
YEGELESLRR FKDDVNEVRN GMECGIGVKN YNDVRAGDMI EVFEIIEIQR TIA
