IF2_CORU7
ID IF2_CORU7 Reviewed; 934 AA.
AC B1VGC2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-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=cu0851;
OS Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=504474;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43042 / DSM 7109;
RX PubMed=18367281; DOI=10.1016/j.jbiotec.2008.02.009;
RA Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A.,
RA Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J.,
RA Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M.,
RA Puehler A.;
RT "The lifestyle of Corynebacterium urealyticum derived from its complete
RT genome sequence established by pyrosequencing.";
RL J. Biotechnol. 136:11-21(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; AM942444; CAQ04811.1; -; Genomic_DNA.
DR RefSeq; WP_012360100.1; NC_010545.1.
DR AlphaFoldDB; B1VGC2; -.
DR SMR; B1VGC2; -.
DR STRING; 504474.cu0851; -.
DR EnsemblBacteria; CAQ04811; CAQ04811; cu0851.
DR GeneID; 60603627; -.
DR KEGG; cur:cu0851; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_0_11; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001727; 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 PRINTS; PR00315; ELONGATNFCT.
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..934
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093777"
FT DOMAIN 430..602
FT /note="tr-type G"
FT REGION 54..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..446
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 464..468
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 489..492
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 543..546
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 579..581
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 54..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 439..446
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 489..493
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 543..546
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 934 AA; 97716 MW; D5F5E794DABBD0B8 CRC64;
MAGKLRVHEL AKKLGVTSKE LLATLKEQGE FVKTASSTVE PPVVKKMKQF YGVAQESKPT
TPPSPLAQAG SVPDSTQRGP KPGAKPAAKP EAAPKPGTAA AKPSAKPSPA AAAKAAPAAK
ATPTPAEAAP KPGQAAAKPA AKPGQKPARA AGKPGPKPGP KPGARPQRVA NNPFSSTTER
PPRPRGGATP GDMPRPGGTR GGAGRGQAPR PGARPAQGQG RGQGTAKPGA ARQGGGRRPS
PAMMPATPSP GQMPAKSAAG FGGGRGRGGR PGGPGGPGGP GGPGPRGGRG GRRGGTAGAF
GRPGGPPRRG RKSKRQKRNE YEAMQAPKVV GGVKLPSGNG EKIRLARGAS LADFADKINA
DAAALVQALF NLGEMVTATQ SVSDETLQLL GDEMDYKVEV VSPEDEDREL LESFDLQFGE
DEGDDEDLAQ RPPVVTVMGH VDHGKTRLLD TIRKENVGSG EAGGITQHIG AYQVSVNMEG
VERPVTFLDT PGHEAFTAMR ARGAKSTDIA ILVVAADDGV MPQTVEAINH AKAAEVPVVV
AVNKIDKPTA QPDKIRGQLT EYGLVPEEYG GDTMFVDISA KQGQNIDQLL EAVLLTADAS
LDLRANPDMD AQGIAIEAHL DRGRGPVATI IVQRGTLRVG DSIVVGDAYG RVRRMIDEHG
NDVQEAGPSR PVQVLGLTSV SGAGDNLLVV DEDRTARQIA DRRDARRRNA LAARSRKRVS
LEDLDEVLKE TSTLNLILKG DNAGTVEALE DALLKIEVDD EVALNIIDRG VGAVTETNVH
LAAASDAVII GFNVRSEGKA TEAANAEGVD IRYYSIIYKA IEEIEAALKG MLKPIYEEKE
IGTAEIRQIF KASAVGLIAG CMVETGKVRR NAKVRLVRDG KVISEDATID SLRREKDDVT
EVSHGYECGM VLSYPNIEVG DRIEAYEMVE VPRD
