IF2_BDEBA
ID IF2_BDEBA Reviewed; 975 AA.
AC Q6MMS6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, 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=Bd1547;
OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS HD100).
OC Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC Bdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=264462;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX PubMed=14752164; DOI=10.1126/science.1093027;
RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA Schuster S.C.;
RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT genomic perspective.";
RL Science 303:689-692(2004).
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; BX842650; CAE79427.1; -; Genomic_DNA.
DR RefSeq; WP_011164029.1; NC_005363.1.
DR AlphaFoldDB; Q6MMS6; -.
DR SMR; Q6MMS6; -.
DR STRING; 264462.Bd1547; -.
DR EnsemblBacteria; CAE79427; CAE79427; Bd1547.
DR KEGG; bba:Bd1547; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_7; -.
DR OrthoDB; 120711at2; -.
DR Proteomes; UP000008080; 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..975
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228172"
FT DOMAIN 469..639
FT /note="tr-type G"
FT REGION 49..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..485
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 503..507
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 525..528
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 579..582
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 615..617
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 51..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 478..485
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 525..529
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 579..582
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 975 AA; 103245 MW; 80CB67F47A8FD156 CRC64;
MSNPKVFEFA KEIGMTPLAL MDKIREWHLP VKSHMAELEP EVLEQIKIKL SGGEKSGDEA
KPKKTAARKA APKKAAVAAP VPEADASSAA AKTPVIRRKK DEVPAEAPKA KVVAKPEGEV
EEAAAAPKTT RVVVKKPAVK AEAEEVEETP EVEAAAPVEE KAPVKAAVKE EAPAPVEKPE
PVVAKEVPAA PVAAAPEAPA PQARKKEVVV GTSGVSSSAT PASAPKRNII GRMDLSRVQS
QAPQRPQGER PAGGFTPRAG GEQRGASASF TGQRPGGFNR PAGGAPTRNI RTGFVAANQP
PEPIVETGAD RGGRDFDKRK RTFGPSAPAA GPAAAGRGAG EKEEVVVSFN AVEFRKREMV
FQPKKKKGLL DRDAMKTQIT TPSAHKRVVK VNNTMKLSDL AMEMGLKAPQ LVRELMKQGV
MANMNMDLDF DTIALIVPEF GWEAQNVFKT ADEVAEQTAF GDLDAAPVTR PPVVTVMGHV
DHGKTSLLDA IRNADVAKGE AGGITQHIGA YSVKIEDGSL ITFLDTPGHE AFTAMRARGA
NATDIAIIVV AADDGMMPQT QEAINHAKAA GVPIIVAVNK IDKPGANPER IKQQLTELEI
VPEEWGGSTI FCEVSALKKT GITELLEQIK LVAEVAELKA NPKRSGTGLV IEAKMEKGKG
PVATLLVKDG TVEVGQYIVA GTMKGRVRSL TNDRGERVQS AGPGIPVEVL GLEAVPAAGD
KFDIVKDEVT ATKVSELRKE QAEKAAATPA AKLSLDEVFA KVKAGDVKEL AIVLKADVHG
SLEAINGMLA KLSTPEVKAR VIHSAVGGIN EGDIVLANTA KGIVLGFNVR PDLGAQAKAK
QMGVDVRTYS IVYELIDQMK AAMGGLLSPD IVEEVLGRAE VRNVFTVPKV GTIAGCFVID
GKVQRNASIR LLRENKIVYE GKIASLKRFK DDAKEVASGY ECGIGIENYN DVKVGDQMEA
FVKKEVAREL EGGAN
