ID Q9AG07_WOLWR Unreviewed; 774 AA.
AC Q9AG07;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 152.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000256|HAMAP-Rule:MF_00100,
GN ECO:0000313|EMBL:AAK31157.1};
GN OrderedLocusNames=WRi_013480 {ECO:0000313|EMBL:ACN96018.1};
OS Wolbachia sp. subsp. Drosophila simulans (strain wRi).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia.
OX NCBI_TaxID=66084 {ECO:0000313|EMBL:AAK31157.1};
RN [1] {ECO:0000313|EMBL:AAK31157.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WRi {ECO:0000313|EMBL:AAK31157.1};
RA Sun L.V., O'Neill S.L.;
RT "Genomic organization of the upstream region of the Wolbachia dnaA gene.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACN96018.1, ECO:0000313|Proteomes:UP000001293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WRi {ECO:0000313|EMBL:ACN96018.1}, and wRi
RC {ECO:0000313|Proteomes:UP000001293};
RX PubMed=19307581; DOI=10.1073/pnas.0810753106;
RA Klasson L., Westberg J., Sapountzis P., Naeslund K., Lutnaes Y.,
RA Darby A.C., Veneti Z., Chen L., Braig H.R., Garrett R., Bourtzis K.,
RA Andersson S.G.;
RT "The mosaic genome structure of the Wolbachia wRi strain infecting
RT Drosophila simulans.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5725-5730(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:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|ARBA:ARBA00007733, ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
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DR EMBL; AF348330; AAK31157.1; -; Genomic_DNA.
DR EMBL; CP001391; ACN96018.1; -; Genomic_DNA.
DR RefSeq; WP_007548684.1; NZ_MKIF01000001.1.
DR AlphaFoldDB; Q9AG07; -.
DR STRING; 66084.WRi_013480; -.
DR KEGG; wri:WRi_013480; -.
DR HOGENOM; CLU_006301_10_2_5; -.
DR Proteomes; UP000001293; 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 {ECO:0000256|HAMAP-Rule:MF_00100};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00100}.
FT DOMAIN 275..446
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 25..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..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:0000256|HAMAP-Rule:MF_00100"
FT BINDING 331..335
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 385..388
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 774 AA; 86037 MW; 8F18366AE4B90185 CRC64;
MNNEDISDKK LTLQGLSKLK LDLNLNSSAS PSTGATVVKK RRKKSHDAEE HNLFDESKLG
SLTEKEQIFR INAVQNAALL KERNQREEKE KTAKEDSNKE TDEKNEADAL SKEINKQVLS
NTHLVEPKED SIDHEDNDKK SFKVNKDIYS KHSKLVIAQA IDEKTEQPPV FKQRFGIRGR
KSKFTKGKNI SREVIIPDKI TIRELSIRMA EDSKSVLKMF KEEVGESYRV DDLVDPDIAC
EIVEKFNHTA KRVSDANKEK DLFFIEGRES LPKKPKPPIV TFMGHVDHGK TSLLDAFRES
NVAERESGGI TQHIGAYQII TKDKQKITFI DTPGHEAFTA MRACGANITN IVVIVVAADD
GIMKQTVEAI NHAKAANVSI IVAINKIDKS EPGDVEKIIN SLPQYDLIPE GLGGDVMIVP
VSAKKKTNLD KLEETILLIA ELMKLEAIED CRALGWVIES KIDKAKGISA TLIVEEGTLK
VGDILVVGTT YSKVRSMVNH LGQREKAALP SAPIEITGLN GVPNAGDKFV VINSEKQARE
IVEYRLELIK KKKEDLGDNN LDIFSRNNSE TEELSVVLKC DVTGSIEAIS SSIDKLGKDQ
VKLNILHKAV GGITDSDVLL AEASSAVILA FNVKVDSKIR DLAKQKGIEI HTYNIIYELI
DDMRMYLTKM LKPVTREVRV GFASVRQIFN VSKAGNIIGC YVSDGVIRKD SLIKVMRGGK
LVHEGKLKAL RRFKDDVKEV GVNFECGVSL EGNIDIKVGD ILEAYQLVQE ERVL
//
