ID   IF2_RICM5               Reviewed;         831 AA.
AC   A8F223;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=RMA_0853;
OS   Rickettsia massiliae (strain Mtu5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=416276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mtu5;
RX   PubMed=17916642; DOI=10.1101/gr.6742107;
RA   Blanc G., Ogata H., Robert C., Audic S., Claverie J.-M., Raoult D.;
RT   "Lateral gene transfer between obligate intracellular bacteria: evidence
RT   from the Rickettsia massiliae genome.";
RL   Genome Res. 17:1657-1664(2007).
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; CP000683; ABV84959.1; -; Genomic_DNA.
DR   RefSeq; WP_012152932.1; NC_009900.1.
DR   AlphaFoldDB; A8F223; -.
DR   SMR; A8F223; -.
DR   PRIDE; A8F223; -.
DR   EnsemblBacteria; ABV84959; ABV84959; RMA_0853.
DR   KEGG; rms:RMA_0853; -.
DR   HOGENOM; CLU_006301_10_2_5; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000001311; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..831
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000057661"
FT   DOMAIN          329..499
FT                   /note="tr-type G"
FT   REGION          338..345
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          363..367
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          385..388
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          439..442
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          475..477
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         338..345
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         385..389
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         439..442
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   831 AA;  91240 MW;  17745C0A529B77AD CRC64;
     MTDNQEIKPK KLTLGNSKLS LNKSFDSLTG AQSFVNANSK TLVEVRKSST GSATTLSLNK
     ERNSLDQTVI DANKEEFNRR LSILKKAAEQ SKLNDPSKIS TLSKLASINQ SANSRIEPLE
     TDKEVEPKQQ NTEENKVEVS AKIVQDDEDI PSQIPKKKED IFVKSPLVGM RTRYGIESEK
     ELDKTADRKI VAPKIKLEEP KKFKKADLFN MLSDDESGSG RTRSLASIKR AREKEKRKLV
     SQAPEKVYRE VTIPEVIGVG DLANAMSERV ADVIKELMKL GILANASQTI DADTAELVAT
     NLGHTVKRVQ ESDVENVLIS DDKVEDLRTR APVVTVMGHV DHGKTSLLDA LKSTDIAAGE
     LGGITQHIGA YRVTLADGRA ITFIDTPGHE AFSEMRSRGA KVTDIVIIVV AADDGIKTQT
     VEAINHAKAA GVPIIVAINK IDKPDIDIER VKNELYVHEI IGEEAGGDVM VIPISALKKI
     NLDKLEEAIL LIAEMQDLKA NPFGAAAGVV IESKIEQGRG TLTTILVQRG TLRNSDIIIA
     GTSYGKVKKM INDKGLEILE ATPSVPVEIQ GLNEVPFAGD KFNVVQNEKQ AKDIAEYRMR
     LAKEKKISIA PRSSLEDLFL KASGNSKIKE LPLIIKGDVQ GSVEAISGSL LKLPSDEIKL
     RILHSGVGPI TESDLSLAHA SSAIIVGFNV RAGANALTAA EKEKVDIRYY SIIYHLIDDI
     KAIMSGMLDP IVREQYIGSA EIRQIFNIIK VGKIAGSYVT KGIIKKRAGV RLLRDNVVIH
     EGKFKTLKRF KDEVKEVREG YECGIAFENY EDIREGDTVE VFELIQEQRQ L