IF2_WOLTR
ID IF2_WOLTR Reviewed; 777 AA.
AC Q5GS99;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Wbm0537;
OS Wolbachia sp. subsp. Brugia malayi (strain TRS).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=292805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRS;
RX PubMed=15780005; DOI=10.1371/journal.pbio.0030121;
RA Foster J., Ganatra M., Kamal I., Ware J., Makarova K., Ivanova N.,
RA Bhattacharyya A., Kapatral V., Kumar S., Posfai J., Vincze T., Ingram J.,
RA Moran L., Lapidus A., Omelchenko M., Kyrpides N., Ghedin E., Wang S.,
RA Goltsman E., Joukov V., Ostrovskaya O., Tsukerman K., Mazur M., Comb D.,
RA Koonin E., Slatko B.;
RT "The Wolbachia genome of Brugia malayi: endosymbiont evolution within a
RT human pathogenic nematode.";
RL PLoS Biol. 3:599-614(2005).
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; AE017321; AAW71125.1; -; Genomic_DNA.
DR RefSeq; WP_011256735.1; NC_006833.1.
DR AlphaFoldDB; Q5GS99; -.
DR SMR; Q5GS99; -.
DR STRING; 292805.Wbm0537; -.
DR EnsemblBacteria; AAW71125; AAW71125; Wbm0537.
DR KEGG; wbm:Wbm0537; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_2_5; -.
DR OMA; LYAWPWP; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000534; 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; 1.
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.
FT CHAIN 1..777
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228260"
FT DOMAIN 279..449
FT /note="tr-type G"
FT REGION 30..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..295
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 313..317
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 334..337
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 388..391
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 425..427
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 98..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 288..295
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 334..338
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 388..391
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 777 AA; 86324 MW; BC0B0EBD48667A21 CRC64;
MNSKDISSKK LTLQGFSKLK LDFNLSSSAS PSMGATIVKK RRRKTHDTEE QDENKLLGSL
TKKEQISRIN AVQNAALLKE RNLKEKEAIV KKDSIVKEDS NEKTNDRDSA TNTSFKETGK
EVLNDVSLVE LIENNTDNED NNKKSLKTNK DIYSKHSKRI IAQSIDDKIE QPSVFKQRFG
IRNRKSEFTK GKNISREVII PDEITIKELS IRMAEDSKSV LKMLKEEMGE NYGVDGLVDP
EVACEIVEKF NHTAKRVSGA NKEKNLFFIE ERESLPKKPK PPIVTFMGHV DHGKTSLLDA
FRESNVAERE LGGITQHIGA YQIITKDKKI TFIDTPGHEA FTAMRACGAN ITNIVVIVVA
ADDGVMKQTI EAMNHAKAAN VSIIVAINKI DRSQSGDVER IISSLPQYDL IPEELGGDVI
VVPVSAKKKI NLDKLEEAIL LIAELMKLEA IEDCRALGWV IESKIDKAKG ISATLIVEEG
TLKVGDMLVV GTAYGKVRSM VNHLGQREKV ALPSSPIEIT GLNGIPNAGD KFVVVSSEKQ
AREIAEYRLE LIKEKKEDLS NNNLDMFSRN DSEVEELSVV LKCDVTGSIE AISNSIDKLG
KDQVKLNILH KAVGGITDSD VLLAEASSAV ILAFNVKVDS KIRDLAKRKG VEIHTYSIIY
ELIDDMRMYL TKMLKPVTRE VRIGSASVRQ IFNVSRVGNI IGCYVSDGVV KKDSLIKVMR
NNKLIYEGKL KALRRFKDNV KEVGTNFECG VSLDGNVDIK VGDILEAHQL VQEERVL
