IF2_CORJK
ID IF2_CORJK Reviewed; 922 AA.
AC Q4JV51;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=jk1142;
OS Corynebacterium jeikeium (strain K411).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=306537;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K411;
RX PubMed=15968079; DOI=10.1128/jb.187.13.4671-4682.2005;
RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT "Complete genome sequence and analysis of the multiresistant nosocomial
RT pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT human skin flora.";
RL J. Bacteriol. 187:4671-4682(2005).
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; CR931997; CAI37306.1; -; Genomic_DNA.
DR RefSeq; WP_011273680.1; NC_007164.1.
DR AlphaFoldDB; Q4JV51; -.
DR SMR; Q4JV51; -.
DR STRING; 306537.jk1142; -.
DR EnsemblBacteria; CAI37306; CAI37306; jk1142.
DR GeneID; 56649492; -.
DR KEGG; cjk:jk1142; -.
DR PATRIC; fig|306537.10.peg.1155; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_0_11; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000545; 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..922
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228187"
FT DOMAIN 418..590
FT /note="tr-type G"
FT REGION 33..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..434
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 452..456
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 477..480
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 531..534
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 567..569
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 86..100
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..158
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 427..434
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 477..481
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 531..534
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 922 AA; 96528 MW; 3400EC66D15F8222 CRC64;
MAGKLRVHEL AKELGVTSKE LLATLKEQGE FVKTASSTVQ PPVVKKMKKH YGVGEESAKE
SATTPSPAAK PGPKPAAKAA PKAAAKPGPK PGPKPGPQPV KNTNPVAGAG TRPTSTVKPG
EKPAPKPGAK PAPKTAAKPT PKPGAKPGPK PGGAKPGAKP GPKPGGRAPR VANNPFSSGA
PAERPAPRPR GGQAGPGDMP RPGSRPGGAK KAGPKPGGAK QGGGRRPSPA MMPSHPNPAQ
MPSKSDNFGG GRGRGGRHGG PGGPGGPGGP GGPRGGRGGR RGGTAGAFGR PGGAPRKGRK
SKRQKRNEYE AMQAPSVVGG VKLPNGKGAK IRLARGASLM DFAEKIKADA AALVQALFNL
GEMVTATQSV SDETLMLLGE EMDYKVEVVS PEDEDRELLE SFDLQFGEDE GEDEDLAQRP
PVVTVMGHVD HGKTRLLDTI RKANVGSGEA GGITQHIGAY QVSVSMEGED RLVTFLDTPG
HEAFTAMRAR GAKSTDIAIL VVAADDGVMP QTVEAINHAK AADIPVVVAV NKIDKEGAQP
DKIRGQLTEY GLIPEEYGGE TMFVDISAKQ GTNIDQLLES VLLTADASLD LRANPDMDAQ
GVAIEAHLDR GRGPVATIIV QRGTLRVGDS IVVGDAYGRV RRMIDEHGND VQEAGPSRPV
QVLGLTSVSG AGDNLLVVDE DRTARQIADR RDARRRNALA ARSRKRVSLE DLDSVLKETN
TLNLILKGDN AGTVEALEDA LLKIEVDDEV DLNIIDRGVG AVTETNVNLA AASDAVIIGF
NVRAEGKATE VANAEGVDIR YYSIIYKAIE EVEAALKGML KPIYEEKQIG TAEIRQIFKA
SSVGLIAGCM VETGKVRRNA QARLVRDGNV VAEKTTIESL RREKDDVTEV SAGYECGMVL
SYPDIQVDDI IEVFELVEVP RT
