IF2_GRAFK
ID IF2_GRAFK Reviewed; 938 AA.
AC A0LXQ1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=GFO_0158;
OS Gramella forsetii (strain KT0803).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Gramella.
OX NCBI_TaxID=411154;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT0803;
RX PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x;
RA Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E.,
RA Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K.,
RA Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I.,
RA Gloeckner F.O.;
RT "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii'
RT reveals adaptations to degradation of polymeric organic matter.";
RL Environ. Microbiol. 8:2201-2213(2006).
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; CU207366; CAL65146.1; -; Genomic_DNA.
DR RefSeq; WP_011708084.1; NC_008571.1.
DR AlphaFoldDB; A0LXQ1; -.
DR SMR; A0LXQ1; -.
DR STRING; 411154.GFO_0158; -.
DR EnsemblBacteria; CAL65146; CAL65146; GFO_0158.
DR KEGG; gfo:GFO_0158; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_0_1_10; -.
DR OMA; VIFAMNK; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000755; 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; 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.
FT CHAIN 1..938
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335474"
FT DOMAIN 434..602
FT /note="tr-type G"
FT REGION 57..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..450
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 468..472
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 490..493
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 544..547
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 580..582
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 57..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 443..450
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 490..494
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 544..547
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 938 AA; 104312 MW; 47AEC832652BAE65 CRC64;
MAEAKTTRLN KVLREFNISL DRAVEYLTSK GYEIDARPTT KISGEIYEVL SDEFETDKSK
KVASKEVGEE RKKEKEELRK EIEEKRKADE EKKEEAVSSR AKLEGPKTVG KIDLDKKPGE
KSKEKEAEAP KEKEKEKETP AKEPVKKAEE SKPTEKPAEK VEEKEDKPKE EKKAEPKKEE
AKPQEAKAEK TKSEEPKSEE TKSEETTEGG ESEEKESDRI ETKYTKLNGP NFTGKKIDLS
QFKKPVKKKE EKKEDDKKDK DRRKKRRRRI SKDVKGGGGN NQRGGAKKGG RTRSKPITKE
EPTEEEVQKQ VRETLEKLQG KSSKGKGAKY RRQKRDEHRQ RSADDLAQQE SDDKILKVTE
FVTVSEVATM MDVQVTQIIS ACMSLGMMVT MNQRLDAETL TIVAEEFDYE VEFTTADVEE
TVEEVEENPE DLVTRAPIVT VMGHVDHGKT SLLDYVRKEN VIAGESGGIT QHIGAYGVKL
EGGQKIAFLD TPGHEAFTAM RARGAQVTDI AIIVIAADDD VMPQTKEAIS HAQAAGVPII
FAINKSDLPT ANPEKIKEKL AAMNLLVEDW GGKIQSHDIS AKTGAGVKEL LEKVLLEAEI
LELKANPKKL AKGTVVEAFL DKGRGYIATI LVQAGTLKIG DYVLAGRNSG KIKAMHDERG
HEVKEAGPST PVSILGLDGA PQAGDTFKVM EDEREAKDIA ARRTQLQREQ NVRTQRHITL
DEIGRRIALG DFKELNIILK GDVDGSVEAL TDSFQKLSTE EIQVNIIHKG VGAITESDVL
LASASDAVII GFNVRPAGNA RQVADKEEID IRTYSIIYDA INDLKDAMEG MLSPELKEEI
TGTAEIRETF KISKIGTIAG CMVTSGTIYR SAGVRLIRDG VVVYTGELSS LKRFKDDVRE
VKKGYDCGMQ VKNYNDIREG DVIEAFREVE VKKTLKSK
