ID   IF2_RICRO               Reviewed;         831 AA.
AC   B0BY61;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=RrIowa_0967;
OS   Rickettsia rickettsii (strain Iowa).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=452659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Iowa;
RX   PubMed=18025092; DOI=10.1128/iai.00952-07;
RA   Ellison D.W., Clark T.R., Sturdevant D.E., Virtaneva K., Porcella S.F.,
RA   Hackstadt T.;
RT   "Genomic comparison of virulent Rickettsia rickettsii Sheila Smith and
RT   avirulent Rickettsia rickettsii Iowa.";
RL   Infect. Immun. 76:542-550(2008).
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; CP000766; ABY72787.1; -; Genomic_DNA.
DR   RefSeq; WP_012150992.1; NC_010263.3.
DR   AlphaFoldDB; B0BY61; -.
DR   SMR; B0BY61; -.
DR   STRING; 452659.RrIowa_0967; -.
DR   PRIDE; B0BY61; -.
DR   EnsemblBacteria; ABY72787; ABY72787; RrIowa_0967.
DR   GeneID; 45539367; -.
DR   KEGG; rrj:RrIowa_0967; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_10_2_5; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000000796; 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..831
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000075615"
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;  91074 MW;  D15D17A8B1248205 CRC64;
     MTDNQEIKPK KLTLGNSKLS LNKSFDSLTG AQSFVNAKSK TLVEVRKSST GSATTLSLNK
     ERNSLDQTVI DANKEEFNRR LSILKKAAEQ SQLNDPSKIS TLSKLASINQ SANSKIEPLE
     TDKEVEQKQQ NTEDNKVEVS AKIVQDDKDI PSQIPKKKEE TFVKSPLVGM RTRYGIESEK
     ELDKTADSKI IAPKIKLEEP KKIKKADLFN MLSDDESGSC RTRSLASIKR AREKEKRKLA
     SQAPEKVYRE VTIPEVIGVG DLANAMSERV ADVIKELMKL GILANASQTI DADTAELVAT
     NLGHTVKRVQ ESDVENVLIS DDKVEDLRTR APVVTVMGHV DHGKTSLLDA LKSTDVAAGE
     LGGITQHIGA YRVTLADGRA ITFIDTPGHE AFSEMRSRGA KVTDIVIIVV AADDGIKTQT
     VEAINHAKAA GVPIIVAINK IDKPDIDIER VKNELYVHEI IGEEVGGDVM IIPISALKKI
     NLDKLEEAIL LIAEMQDLKA NPFGSAAGVV IESKIEQGRG TLTTILVQRG TLRNSDIIIA
     GTAYGKVKKM TNDKGLEIVE ATPSVPVEIQ GLNEVPFAGD KFNIVQNEKQ AKDIAEYRMR
     LAKEKKISIA PRSSLEDLFL KASGNSKIKE LPLIIKGDVQ GSVEAISGSL LKLPSDEIKL
     RILHSGVGPI TESDVSLAHA SSAIIVSFNV RAGANALTAA EKEKVDIRYY SIIYHLIDDI
     KAIMSGMLEP IVREQYIGSA EIRQIFNITK VGKIAGSYVT KGIIKKGAGV RLLRDNVVIH
     EGKLKTLKRF KDEVKEVREG YECGIAFENY EDIREGDTVE VFELIQEQRQ L