ID IF2_ALLAM Reviewed; 926 AA.
AC B9JYK6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Avi_0169;
OS Allorhizobium ampelinum (strain ATCC BAA-846 / DSM 112012 / S4)
OS (Agrobacterium vitis (strain S4)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Allorhizobium;
OC Allorhizobium ampelinum.
OX NCBI_TaxID=311402;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-846 / DSM 112012 / S4;
RX PubMed=19251847; DOI=10.1128/jb.01779-08;
RA Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K.,
RA Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., Otten L.,
RA Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., Du Z., Ewing A.,
RA Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., Miller N.M.,
RA Norton S., Chen Q., Phoolcharoen W., Ohlin V., Ondrusek D., Pride N.,
RA Stricklin S.L., Sun J., Wheeler C., Wilson L., Zhu H., Wood D.W.;
RT "Genome sequences of three Agrobacterium biovars help elucidate the
RT evolution of multichromosome genomes in bacteria.";
RL J. Bacteriol. 191:2501-2511(2009).
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; CP000633; ACM35102.1; -; Genomic_DNA.
DR RefSeq; WP_012654632.1; NC_011989.1.
DR AlphaFoldDB; B9JYK6; -.
DR SMR; B9JYK6; -.
DR STRING; 311402.Avi_0169; -.
DR KEGG; avi:Avi_0169; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_0_5; -.
DR Proteomes; UP000001596; Chromosome 1.
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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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; 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; IPR004161; EFTu-like_2.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
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; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 1.
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.
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..926
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000118743"
FT DOMAIN 424..591
FT /note="tr-type G"
FT REGION 1..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..440
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 458..462
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 479..482
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 533..536
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 569..571
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 13..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..97
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 433..440
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 479..483
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 533..536
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 926 AA; 100386 MW; 10CD30124A7A288F CRC64;
MTDSKDDKTL SVTGKKTLTL KPTGVNQGTV RQDMGRGRTK AVVVETRKRR PTRPEDERAG
QPQGRVGDDA PATAAAAPVQ TPAPVQAPAP VAAAPQAPRP AAPAQRVQQT NQYSQQRHPG
QQNRPQASSQ PSRQPDRPRG AVLHDLSASE MDARRRALAE AQVREVEDAK RRAEEEVRRQ
AEEVERQRLA ALEAIRQAEE DKARALEAKN APEPVAEPVA PVAETPRAAD PAPRAPSPAG
AKPAAGAPAP SFVRGRKPEG EDDENRGPAR GGPVRGKVVR PEPAKVPARP KTEDERRRGK
LTVTTAAVDE DGNARGRSLS AMRRRQEKFR RSQMQEPREK VMREVVLPET ITIQELSQRM
SERAVDVIKY LMKEGQMMKP GDVIDADLAE LIATEFGHTV KRVSESDVEE GIFDVKDDAG
EMVSRPPVVT IMGHVDHGKT SLLDAIRQTS VVSGEAGGIT QHIGAYQVEQ NGHKITFIDT
PGHAAFTAMR ARGAQATDIA ILVVAADDSV MPQTIESIHH AKAANVPIIV AINKIDKHEA
NPEKVRQQLL QHEVFVESMG GEVLDVEVSA KNKLNLDKLL EAVLLQAEIL DLKADPSRTA
EGLVIEAQLD RGRGSVATVL VQKGTLRPGQ IIVAGDQWGR VRALVNDKGG HVKEAGPAMP
VEVLGLSGTP AAGDKFAVVE SEARAREISE YRQRLARDKA AARQSGQRGS LEQMMSKLQD
TGFKEFPLVI KADVQGSVEA IVAALDKLGT DEVRARIVHS GAGAITESDI SLAEASNAAI
IGFNVRANVQ ARAASERTGT EIRYYNIIYD LVDDVKAAMS GLLSPERRET FLGNAEILEV
FNITKTGKVA GCRVVEGKVE RGAGVRLVRD NVVIHEGKLK TLKRFKDEVA DVPMGQECGM
AFENYEDIRA GDTIECFRVE HITRTL
//
