ID IF2_WOLPM Reviewed; 774 AA.
AC Q73FL0;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=WD_1318;
OS Wolbachia pipientis wMel.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia.
OX NCBI_TaxID=163164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15024419; DOI=10.1371/journal.pbio.0020069;
RA Wu M., Sun L.V., Vamathevan J.J., Riegler M., DeBoy R.T., Brownlie J.C.,
RA McGraw E.A., Martin W., Esser C., Ahmadinejad N., Wiegand C., Madupu R.,
RA Beanan M.J., Brinkac L.M., Daugherty S.C., Durkin A.S., Kolonay J.F.,
RA Nelson W.C., Mohamoud Y., Lee P., Berry K.J., Young M.B., Utterback T.R.,
RA Weidman J.F., Nierman W.C., Paulsen I.T., Nelson K.E., Tettelin H.,
RA O'Neill S.L., Eisen J.A.;
RT "Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a
RT streamlined genome overrun by mobile genetic elements.";
RL PLoS Biol. 2:327-341(2004).
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; AE017196; AAS14960.1; -; Genomic_DNA.
DR RefSeq; WP_010963178.1; NZ_JAIUXN010000015.1.
DR AlphaFoldDB; Q73FL0; -.
DR SMR; Q73FL0; -.
DR EnsemblBacteria; AAS14960; AAS14960; WD_1318.
DR GeneID; 70036780; -.
DR KEGG; wol:WD_1318; -.
DR eggNOG; COG0532; Bacteria.
DR Proteomes; UP000008215; 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; 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; 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; PF11987; IF-2; 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.
FT CHAIN 1..774
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228259"
FT DOMAIN 275..446
FT /note="tr-type G"
FT REGION 25..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..291
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 309..313
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 331..334
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 385..388
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 422..424
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 82..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 284..291
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 331..335
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 385..388
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 774 AA; 86182 MW; 8F2E18001A0C7199 CRC64;
MNNEDISDKK LTLQGLSKLK LDLNLNSSAS PSTGATVVKK RRKKSHDAEE HNLFDESKLC
SLTEKEQIFR INAVQNAALL KERNQREEKE KTAKEDSNKE IDEKNEADAL SKEINKQVLS
NTHLVEPKED SIDHEDNDKK SFKVNKDIYS KHSKLVIAQA IDEKTEQPPV FKQRFGIRGR
KSKFTKGKNI SREVIIPDKI TIRELSIRMA EDSKSVLKMF KEEVGESYRV DDLVDPDIAC
EIVEKFNHTA KRVSDTNREK DLFFIEGRES LPKKPKPPIV TFMGHVDHGK TSLLDAFRES
NVAERESGGI TQHIGAYQIT TKDKQKITFI DTPGHEAFTA MRARGANITN IVVIVVAADD
GIMKQTVEAI NHAKAANVSI IVAINKIDKS EPGDVEKIIN SLPQYDLIPE GLGGDVMIMP
VSAKKKTNLD KLEEAILLIA ELMKLEAIED CRALGWVIES KIDKAKGISA TLIVEEGTLK
VGDILVVGTT YSKVRSMVNH LGQREKAALP SAPIEITGLN GVPNAGDKFV VVNSEKQARE
IVEYRLELIK KKKEDLGDNN LDIFSRNNSE TEELSVVLKC DVTGSIEAIS SSIDKLGKDQ
VKLNILHKAV GGITDSDVLL AEASSAVILA FNVKVDSKIR DLAKQKGIEI HTYNIIYELI
DDMRMYLTKM LKPVTREVRV GFASVRQIFN VSKAGNIIGC YVSDGVIRKD SLIKVMRGGK
LVHEGKLKAL RRFKDDIKEV GVNFECGVSL EGNVDIKVGD ILEAYQLVQE ERVL
//
