ID I7IAG9_9RICK Unreviewed; 772 AA.
AC I7IAG9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
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 ORFNames=wOo_08260 {ECO:0000313|EMBL:CCF78374.1};
OS Wolbachia endosymbiont of Onchocerca ochengi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia.
OX NCBI_TaxID=100901 {ECO:0000313|EMBL:CCF78374.1, ECO:0000313|Proteomes:UP000007516};
RN [1] {ECO:0000313|EMBL:CCF78374.1, ECO:0000313|Proteomes:UP000007516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Adamawa_Cameroon {ECO:0000313|Proteomes:UP000007516};
RX PubMed=22919073; DOI=10.1101/gr.138420.112;
RA Darby A.C., Armstrong S.D., Bah G.S., Kaur G., Hughes M.A., Kay S.M.,
RA Koldkaer P., Rainbow L., Radford A.D., Blaxter M.L., Tanya V.N.,
RA Trees A.J., Cordaux R., Wastling J.M., Makepeace B.L.;
RT "Analysis of gene expression from the Wolbachia genome of a filarial
RT nematode supports both metabolic and defensive roles within the
RT symbiosis.";
RL Genome Res. 22:2467-2477(2012).
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; HE660029; CCF78374.1; -; Genomic_DNA.
DR RefSeq; WP_014869159.1; NC_018267.1.
DR AlphaFoldDB; I7IAG9; -.
DR STRING; 100901.wOo_08260; -.
DR KEGG; woo:wOo_08260; -.
DR PATRIC; fig|100901.6.peg.676; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_5; -.
DR Proteomes; UP000007516; 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}; Reference proteome {ECO:0000313|Proteomes:UP000007516}.
FT DOMAIN 273..444
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 282..289
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 329..333
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 383..386
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 772 AA; 86023 MW; B98295E96D25E355 CRC64;
MNNEEGISSK KLTLQGFNKL KFGLDLSYPV SPNIGATIVK KRRRKIREPE GQSESKLGSL
TEKEQIFRIN AVQNAVLLKE KNLKKEKEVI TKEDNNRKID EDSISCSLLK ENKEKGSSGV
SLVKLMEERI DDEFVNKKSL KTNKDVYSKY SKLIIAQSID DKVEQTLVFK QRFGIRNKRS
KFIKGKNISR EVIIPDKITI KELSIRMAEE SKGVLKMLEE EIGESCKVDD FVNPDIACKI
VEKFNHVAKR VSNVDKERDL LFVENKKSLP KKPKPPVVTF MGHVDHGKTS LLDAFRDSNI
AEKESGGITQ HIGAYQIVTK NKQKITFIDT PGHEAFTAMR ACGANITDIV VIVIAADDGV
MKQTIEAINH AKSANVSIIV AINKIDRSQP GDVERIISSL PRYGLIPEEL GGDVIVVPIS
AKKRINLDKL EEAILLVAEL MKLEAIEDCR ALGWVIESKI DKAKGISATL IVEEGTLKVG
DILVLGTTYG KVRNMVNHFG ERENIALPST AVEITGLNGI PNAGDKFVVV SSEKQTREII
EYRLDLVRKK KGNSNDNNPN IFNHGDSKIE EISLLLKCDV TGSIEAILNS INKLSKNQVK
LNILHKAVGG ITDSDVLLAE ASNAIILAFN VKTDSKIRDM AKQKGVEIHT YNIIYELIDD
MKMYLTKILK PITREVRIGS ASVRQIFSTS KASNIIGCYI SDGVAKKDSL IKVMRNSKLI
CKGKLKALRR FKDDVKEVVT DFECGMSLDG NVDVKVGDIL EVYQLVQEER IL
//
