IF2_ARTS2
ID IF2_ARTS2 Reviewed; 968 AA.
AC A0JUU0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Arth_1416;
OS Arthrobacter sp. (strain FB24).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=290399;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB24;
RX PubMed=24501649; DOI=10.4056/sigs.4438185;
RA Nakatsu C.H., Barabote R., Thompson S., Bruce D., Detter C., Brettin T.,
RA Han C., Beasley F., Chen W., Konopka A., Xie G.;
RT "Complete genome sequence of Arthrobacter sp. strain FB24.";
RL Stand. Genomic Sci. 9:106-116(2013).
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; CP000454; ABK02810.1; -; Genomic_DNA.
DR RefSeq; WP_011691277.1; NC_008541.1.
DR AlphaFoldDB; A0JUU0; -.
DR SMR; A0JUU0; -.
DR STRING; 290399.Arth_1416; -.
DR PRIDE; A0JUU0; -.
DR EnsemblBacteria; ABK02810; ABK02810; Arth_1416.
DR KEGG; art:Arth_1416; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_1_11; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000754; 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.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..968
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335457"
FT DOMAIN 461..632
FT /note="tr-type G"
FT REGION 51..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..477
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 495..499
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 520..523
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 574..577
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 610..612
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 71..89
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 470..477
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 520..524
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 574..577
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 968 AA; 99772 MW; 91D9B184E38A3095 CRC64;
MAKVRVHELA KELGITSKDA VTKLQELGEF VRSASSTIEA PVVRKLRNAY PAAGASKSEA
PAAAPKAPAS PAATRPAPAP GPAAPKAPEP KAEAPAAASA PSAPAPAAPA PAAPAAAASA
PSAPAPAAPS TGAKPGARPA PKAEAPAAPA RSGGQGSAPR PGGPRPGNNP FATSQGMPRG
RGGDNERPPR PGNNPFAPSQ GMPRPGGSRT EGERPGGPRP AAGAGGPRPG APRPGGTQGA
RPGAPRPAGA PGARPGAGGG NRPTPGMMPN RTERPAPAGA GRPGGGGRGP GRPGGAPGTG
GAPGAGGGAP AGGGFGKGGR GRGGTQGAFG KGGAGRGKQR KSKRAKRQEL EQMSAPSLGG
VSVPRGDGNT VVRLRRGSSI TDFADKIEAN PAALVTVLFH LGEMATATQS LDEETFALLG
EELGYKLQVV SPEDEERELL SGFDIDFDAE LEAEGDEELE ARPPVVTVMG HVDHGKTRLL
DAIRNSDVVA GEHGGITQHI GAYQITTEHE GAERKITFID TPGHEAFTAM RARGAKVTDI
AILVVAADDG VMPQTVEALN HAQAANVPIV VAVNKIDKEG ANPDKVRGQL TEYGLVPEEY
GGDTMFVEVS ARQNLNIDEL LEAVLLTADA ALDMRANPNK DARGIAIEAN LDKGRGAVAT
VLVQSGTLHV GDTIVAGTAH GRVRAMFDDD GSVLTEAGPS RPVQVLGLSN VPRAGDTFFV
TADERTARQI AEKREAADRN AALAKRRKRI SLEDFDQAVA EGKIDTLNLI LKGDVSGAVE
ALEDALLKID VGEGVQLRVI HRGVGAITQN DVNLATVDSA VIIGFNVKPA ERVAELADRE
GVDMRFYSVI YAAIDDIEMA LKGMLKPEYE EVQLGTAEVR EVFRSSKFGN IAGSIVRSGV
IRRNSKARIS RDGKIIGDNL TVETLKRFKD DATEVRTDFE CGIGLGSYND INEGDIIETF
EMREKPRV
