ID   IF2_RICPR               Reviewed;         831 AA.
AC   Q9ZCZ8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Translation initiation factor IF-2;
GN   Name=infB; OrderedLocusNames=RP552;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ235272; CAA15001.1; -; Genomic_DNA.
DR   PIR; G71659; G71659.
DR   RefSeq; NP_220924.1; NC_000963.1.
DR   RefSeq; WP_004599046.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZCZ8; -.
DR   SMR; Q9ZCZ8; -.
DR   STRING; 272947.RP552; -.
DR   EnsemblBacteria; CAA15001; CAA15001; CAA15001.
DR   GeneID; 57569675; -.
DR   KEGG; rpr:RP552; -.
DR   PATRIC; fig|272947.5.peg.565; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_10_2_5; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000002480; 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; Reference proteome.
FT   CHAIN           1..831
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000137244"
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:0000250"
FT   BINDING         385..389
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         439..442
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   831 AA;  91275 MW;  B7945CB26D87C7D0 CRC64;
     MTDNQEIKPK KLTLGNSKLL LNKSFDSLTG AQSFVNAKSK TLVEVRKSSI GSTTTISLNK
     ERNSLDQSVI DSNKEEFNRR LSILKKAAEQ SKLHDPAQIS TLSKLASINQ SINSKNEQSI
     TDKAVEQKHQ NIEDNKVEIA AKIVQDNENI SSQIPKKKKE TLAKSVLVGM RTRYGIEEEP
     ALEKTVDNKV VVPKIKLEES KKFKKADLFN MLSDDENGSG RTRSLASIKR AREKEKRKLV
     SQVPEKVYRE VTIPEVIGVG DLANAMSERV ADVIKELMKL GILANASQTI DADTAELVAT
     NLGHTVTRVQ ESDVENILIN DDKVEDLRTR APVVTVMGHV DHGKTSLLDA LKSTDIAAGE
     LGGITQHIGA YRVTLADSKA ITFIDTPGHE AFSEMRSRGA KVTDIVIIVV AADDGIKTQT
     VEAINHAKAA GVPIIVAINK IDKPDIDIER IKNELYVHEI IGEEAGGDVI FIPISALKKI
     NLDKLEEAIL LISEMQDLKA SPFGLASGVV IESKIEKGRG TLTTILVQRG TLRNGDIIIA
     GTSYGKVKKM INDKGREILE ATPSVPVEIQ GLNEVPFAGD QFNVVQNEKQ AKDIAEYRIR
     LAKEKKISVA SRSSLEELLL KASGNSKIKE LPLIIKCDVQ GSIEAISGSL LKLPSDEIKL
     RILHSGVGPI TESDVSLAHV SSAIVVGFNV RAWANALTAA EKTKVDIRYY SIIYNLIDDV
     KAIMSGMLEP IVREQYIGSV EIRQIFNITK IGKIAGSYVT KGIIKKGAGV RLLRDNVVIH
     AGKLKTLKRF KDEVKEVREG YECGIAFENY EDIREGDTVE VFELVQEQRQ L