ID IF2_SALG2 Reviewed; 892 AA.
AC B5REN6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SG3177;
OS Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550538;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=287/91 / NCTC 13346;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(2008).
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; AM933173; CAR38976.1; -; Genomic_DNA.
DR RefSeq; WP_000133061.1; NC_011274.1.
DR AlphaFoldDB; B5REN6; -.
DR SMR; B5REN6; -.
DR KEGG; seg:SG3177; -.
DR HOGENOM; CLU_006301_6_3_6; -.
DR Proteomes; UP000008321; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.56.50; Putative DNA-binding domain, N-terminal subdomain of bacterial translation initiation factor IF2; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR004161; EFTu-like_2.
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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
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..892
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093820"
FT DOMAIN 391..560
FT /note="tr-type G"
FT REGION 93..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..407
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 425..429
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 446..449
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 500..503
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 536..538
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 93..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 265..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 400..407
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 446..450
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 500..503
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 892 AA; 97414 MW; DD5BEA707A7E2D49 CRC64;
MTDVTLKALA AERQVSVDRL VQQFADAGIR KSADDSVSAQ EKQTLLAHLN REAVSGPDKL
TLQRKTRSTL NIPGTGGKSK SVQIEVRKKR IFVKRDPQEA ERLAAEEQAQ REAEEQARRE
AEEQAKREAQ QKAEREAAEQ AKREAAEKAK REAAEKDKVS NQQTDDMTKT AQAEKARREN
EAAELKRKAE EEARRKLEEE ARRVAEEARR MAEENKWTAT PEPVEDTSDY HVTTSQHARQ
AEDENDREVE GGRGRGRNAK AARPAKKGKH AESKADREEA RAAVRGGKGG KRKGSSLQQG
FQKPAQAVNR DVVIGETITV GELANKMAVK GSQVIKAMMK LGAMATINQV IDQETAQLVA
EEMGHKVILR RENELEEAVM SDRDTGAAAE PRAPVVTIMG HVDHGKTSLL DYIRSTKVAS
GEAGGITQHI GAYHVETDNG MITFLDTPGH AAFTSMRARG AQATDIVVLV VAADDGVMPQ
TIEAIQHAKA AGVPVVVAVN KIDKPEADPD RVKNELSQYG ILPEEWGGES QFVHVSAKAG
TGIDELLDAI LLQAEVLELK AVRKGMASGA VIESFLDKGR GPVATVLVRE GTLHKGDIVL
CGFEYGRVRA MRNELGQEVL EAGPSIPVEI LGLSGVPAAG DEVTVVRDEK KAREVALYRQ
GKFREVKLAR QQKSKLENMF ANMTEGEVHE VNIVLKADVQ GSVEAISDSL LKLSTDEVKV
KIIGSGVGGI TETDATLAAA SNAILVGFNV RADASARKVI ESESLDLRYY SVIYNLIDEV
KAAMSGMLSP ELKQQIIGLA EVRDVFKSPK FGAIAGCMVT EGTIKRHNPI RVLRDNVVIY
EGELESLRRF KDDVNEVRNG MECGIGVKNY NDVRVGDMIE VFEIIEIQRT IA
//
