IF2_ROSS1
ID IF2_ROSS1 Reviewed; 729 AA.
AC A5UZQ2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=RoseRS_3751;
OS Roseiflexus sp. (strain RS-1).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Roseiflexus.
OX NCBI_TaxID=357808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.;
RT "Complete sequence of Roseiflexus sp. RS-1.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000686; ABQ92105.1; -; Genomic_DNA.
DR RefSeq; WP_011958447.1; NC_009523.1.
DR AlphaFoldDB; A5UZQ2; -.
DR SMR; A5UZQ2; -.
DR STRING; 357808.RoseRS_3751; -.
DR PRIDE; A5UZQ2; -.
DR EnsemblBacteria; ABQ92105; ABQ92105; RoseRS_3751.
DR KEGG; rrs:RoseRS_3751; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_2_0; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000006554; 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..729
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335505"
FT DOMAIN 229..396
FT /note="tr-type G"
FT REGION 20..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..245
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 263..267
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 284..287
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 338..341
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 374..376
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 90..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 238..245
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 284..288
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 338..341
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 729 AA; 77423 MW; 1223C8A891620302 CRC64;
MSDMQISGYQ SAINARHYIQ FAGGGRGPGN PGGGRGPGNP GGGRGPGSPG GGRGPGSPGG
GRGPGSPGGG RGPGNPGGGR GPGGGRGGGR GGDGRRRDES FVENEGGRGN RSGRTTSTAT
TARTPGGLAR PTTTVRAPVR PKGPIALPVT MTVREFSEAT GVGASEILKA LLKAGVVANI
NQQIDYETAA VIAADFGIET VEYVPPQLEG VVENIRDVLA AQDPKDMKPR PPVVTIMGHV
DHGKTKLLDA IRSTRVAESE AGGITQHIGA YQVELHGRKI TFLDTPGHEA FTAMRARGAQ
VTDIVVLVVA ADDGVMPQTL EAISHVKAAG VPMIVAINKI DAPNANPDRV RQQLANAGVI
VEQFGGDVPS VEVSAKLKKN IDGLLEIILL VADLNEYKAN PNAPAVGTII EAEMDRTRGP
VATVLVQNGT LRLEDNVLVG STTGTIRTMF NDAGKRLRFA EPATPVVILG LHDVPQAGDI
LQVMPDLAVA REIALQRQRK QRLEAMATSR GVSLDGLFSS IQQGKIKELN IILKADVQGS
IGAIEHALSQ LNTDEVQIRI IHRGTGTITE SDVNLAIASH AIIIGFNARP DPAARRQAEQ
YGVDIRFYNI IYQLTEDIKK AMIGMLEPEY REVTEGFAEV RNTFRLPTRE IVAGLYVTEG
KISRQYNVRV LRNGVVLHDG KIASLKRFKD DVREVQAGYE CGLIVEGFND ITPGDTMEFY
RRERVERTV
