IF2_BORGP
ID IF2_BORGP Reviewed; 883 AA.
AC Q65ZX2;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BG0827;
OS Borrelia garinii subsp. bavariensis (strain ATCC BAA-2496 / DSM 23469 /
OS PBi) (Borrelia bavariensis).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=290434;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2496 / DSM 23469 / PBi;
RX PubMed=15547252; DOI=10.1093/nar/gkh953;
RA Gloeckner G., Lehmann R., Romualdi A., Pradella S., Schulte-Spechtel U.,
RA Schilhabel M., Wilske B., Suehnel J., Platzer M.;
RT "Comparative analysis of the Borrelia garinii genome.";
RL Nucleic Acids Res. 32:6038-6046(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; CP000013; AAU07649.1; -; Genomic_DNA.
DR RefSeq; WP_011194094.1; NZ_CP028872.1.
DR AlphaFoldDB; Q65ZX2; -.
DR SMR; Q65ZX2; -.
DR STRING; 290434.BG0827; -.
DR EnsemblBacteria; AAU07649; AAU07649; BG0827.
DR KEGG; bga:BG0827; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_1_1_12; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 42112at2; -.
DR Proteomes; UP000002276; 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..883
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228174"
FT DOMAIN 381..554
FT /note="tr-type G"
FT REGION 32..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..397
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 415..419
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 436..439
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 490..493
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 526..528
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 390..397
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 436..440
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 490..493
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 883 AA; 98162 MW; B682AB5D931F5102 CRC64;
MSENIDDIKN EDSKKIKIIK LRKKVVKIVT HNDLNGKNNS NSSINLDKHN NKVEYSQNRD
NRAGGYSQNR DNRTGGYSQN RDNRTGGYSQ NRDNRTGGYS QNRDNRTGGY SQNRDNRTGG
YSQNRDNRTG GYSQNRDNRT GGYSQNRDNR TGGYSQNRDN RTGGYSQNRD NRTGGYSQNR
DNRTGGYSQN RDSFPSQYQV STKKTYVGKN TSQNKYTTTP MSFRRVIKAK VPSIVSSASS
VDSENIKELN RKLGEKKKQQ QESQKSYKRK KAETESKTIE QKVFEQLQKK KRENLANPIP
KSIDIMGSIT VSDLARKMNL KSSDLIAKLM ALGVMVTINE KIDSDTATIL VEEYGSKVNV
VSIYDETFIE EEVEDQSKRI EKPPVITIMG HVDHGKTKLL SVLQNIDINQ TESGGITQHI
GAYTIVYNGR EITFLDTPGH EAFTMMRSRG AQVTDIVVLV VSAIDGVMPQ TIEAINHAKE
ANVPIIVAIN KIDLPDSNPD KVKHQLSEYD LVPEDWGGDT IFVLISALKN IGISELLDMI
LLQSDMMLLK ANPSKRAIGK VLDAKIDLGR GIVCSVIIED GTLYIGDSFV GGVCYGKVKA
LISDKGVSVK SVGPAKAISV LGFSSMPQAG DPFQVTKTEK EAKLISSKRQ DLKKYESSKN
VKKVTMLNLY DSIKEGALKE LKIILKADVQ GSVEALKNSL EKLTNDEVRV RVVHSSAGVI
TETDISFASA SDAIVIGFHV RPTSKAQILA DQEKVEIRKY NVIYDAISDV KSVLEGMLEP
DVEQQFIGFA EVRAVINVPK VGVIAGCYVS RGIIKRDAIT NVMRDGLQIH SGKISSLKRF
KDDVKEVAEQ YECGIMIDNY ANIKEGDIIE AFEVKKIKKT FKT
