ID IF2_CORGL Reviewed; 1004 AA.
AC Q8NP40;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 138.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=Cgl1985, cg2176;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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; BA000036; BAB99378.1; -; Genomic_DNA.
DR EMBL; BX927153; CAF20326.1; -; Genomic_DNA.
DR RefSeq; NP_601191.1; NC_003450.3.
DR RefSeq; WP_011014802.1; NC_003450.3.
DR RefSeq; WP_011265855.1; NC_006958.1.
DR AlphaFoldDB; Q8NP40; -.
DR SMR; Q8NP40; -.
DR STRING; 196627.cg2176; -.
DR KEGG; cgb:cg2176; -.
DR KEGG; cgl:Cgl1985; -.
DR PATRIC; fig|196627.13.peg.1924; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_0_11; -.
DR OrthoDB; 9811804at2; -.
DR BioCyc; CORYNE:G18NG-11577-MONOMER; -.
DR Proteomes; UP000000582; Chromosome.
DR Proteomes; UP000001009; 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; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 1.10.10.2480; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; 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; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
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..1004
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137197"
FT DOMAIN 499..671
FT /note="tr-type G"
FT REGION 36..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..515
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 533..537
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 558..561
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 612..615
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 648..650
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 76..96
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..196
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..234
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 508..515
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 558..562
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 612..615
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT CONFLICT 81
FT /note="P -> R (in Ref. 2; CAF20326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1004 AA; 103413 MW; FC159DE2AE29283F CRC64;
MPGKLRVHEL AKQLGITSKE LLATLKDKGE FVKTASSTIE PPVVKRMQEH YGSSGSDKSD
TAAKPAAAKP AAPKPAASAA PKPGAPAKPA APAAKPAPAA PSAASAAKPG AAPKPGVQAK
PAAAAKPGAP AKPAAPAAPS AAKSGSAPKP AAAAKPAFSG PTPGDAAKKA EPAAKPGAEA
PRPGGMPRPM GKPAPKPGAR APRVANNPFS TGGGERPAPR PGGGPRPGGG PRPGGGPRPQ
GQGRPGGQRD GQRDGQRDGQ GNRGGQRQGA GAGGPRPQGG PRPQGGSRPQ GGSAQGAQGA
PSQERQGGGR RPSPAMMPPT PGQMPAKAPG KGGRGGQAGG GAGGGFNRGG GTGGGAGRGG
RRGGTAGAFG RPGGAPRRGR KSKRQKRNEY ESMQAPNVIG GVRLPDGKGA TIRLARGASL
ADFADKIGAD AAALVQALFN LGEMVTATAS VSDETLQLLG EEMNYKVQVV SPEDEDRELL
ESFDLQFGED EGGEADLAKR PPVVTVMGHV DHGKTRLLDT IRKANVGSDE AGGITQGIGA
YQVKVNVEDT ERTITFLDTP GHEAFTAMRA RGAKSTDIAV LVVAADDGVM PQTVEAINHA
KAADVPIVVA VNKIDKPEAS PEKIRGQLTE YGLIPEEYGG DTIFVDISAK QGLNIDELLA
SVCLTADAEL DLVANPEMDA QGVAIEAHLD RGRGPVATVI VQRGTLRVGD SIVAGDTYGR
VRRMVDEYGR DVEEAGPSRP VQVQGLNGVP GAGDNLLVVE DDRIARQIAN QRNARKRNAL
AARSRKRVSL EDLDSVLKEH STLNLILKGD NAGSVEALEE ALLKIEMDDE VQLNIIDRGV
GAVTQTNVTL AAASDAVIIA FNVRAEGKAT EEANAEGVDV RYYTIIYRAI EEVEAALKGM
LKPIYEERVI GHAEIRAIFK ASSVGLIAGC MVEDGKVRRN ATVRIIRDGN VIAENAKIVS
LRREKDDATE VSAGYECGMV LSYPDISVDD KIEVYEMVEV PREA
//
