IF2_RICFE
ID IF2_RICFE Reviewed; 829 AA.
AC Q4UL51;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=RF_0871;
OS Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=315456;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1525 / URRWXCal2;
RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA Parinello H., Claverie J.-M., Raoult D.;
RT "The genome sequence of Rickettsia felis identifies the first putative
RT conjugative plasmid in an obligate intracellular parasite.";
RL PLoS Biol. 3:1-12(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; CP000053; AAY61722.1; -; Genomic_DNA.
DR RefSeq; WP_011271199.1; NC_007109.1.
DR AlphaFoldDB; Q4UL51; -.
DR SMR; Q4UL51; -.
DR STRING; 315456.RF_0871; -.
DR EnsemblBacteria; AAY61722; AAY61722; RF_0871.
DR KEGG; rfe:RF_0871; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_2_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000008548; 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..829
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228237"
FT DOMAIN 327..497
FT /note="tr-type G"
FT REGION 128..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..343
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 361..365
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 383..386
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 437..440
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 473..475
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 336..343
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 383..387
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 437..440
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 829 AA; 90738 MW; CDD151634C3413C7 CRC64;
MTDNQEIKPK KLTLGNSKLS LNKSFDSLTG AQSFVNAKSK TLVEVRKSST GSTTTLSLNK
ERNSLDQTAI DANKEEFNRR LSILKKAAEQ SKLNDPSQIS TLSKLASINQ SANSKIETLE
TEVEQKQQNA EEEKVEASAK TVQNNEDIQP QTSKKKEETF VKSPLVGMRT RYGIESEKEL
DKTVDNKVVA PKIKLEEPKK FKKADLFNML GDDESGSGRT RSLASIKRAR EKEKRKLVSQ
APEKVYREVT IPEVIGVGDL ANAMSERVAD VIKELMKLGI LANASQTIDA DTAELVATNL
GHTVKRVQES DVENVLISDD KVEDLRTRAP VVTVMGHVDH GKTSLLDALK STDIAASETG
GITQHIGAYR VTIADDRAIT FIDTPGHEAF SEMRSRGAKV TDIVIIVVAA DDGIKTQTVE
AINHAKAAGV PIIVAINKID KPDIDIERVK NELYVHEIIG EEAGGDVMVI PISALKKINL
DKLEEAILLI AEMQDLKASP FGSAAGVVIE SKIEKGRGTL TTILVQRGTL RNGDIIIAGS
SYGKVKKMTN DKGLEIVEAT PSVPVEIQGL NEVPFAGDKF NVVQNEKQAK DIAEYRMRLA
KEKKISIAPR SSLEDLFLKA SGNSKIKELP LIIKGDVQGS VEAISGSLLK LPSDEIKLRI
LHSGVGPITE SDVSLAHASS AIIVGFNVRA GANALTAAEK EKVDIRYYSI IYNLIDDVKA
IMSGMLDPIV REQYIGSVEI RQIFNITKVG KIAGSYVTKG IIKKGAGVRL LRDNVVIHEG
KLKTLKRFKD EVKEVREGYE CGIAFENYED IREGDTVEVF ELVQEQRQL
