IF2_CHLSY
ID IF2_CHLSY Reviewed; 745 AA.
AC B9LBJ2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Chy400_3259;
OS Chloroflexus aurantiacus (strain ATCC 29364 / DSM 637 / Y-400-fl).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=480224;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29364 / DSM 637 / Y-400-fl;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Kiss H., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Bryant D.A., Richardson P.;
RT "Complete sequence of Chloroflexus sp. Y-400-fl.";
RL Submitted (JAN-2009) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001364; ACM54637.1; -; Genomic_DNA.
DR RefSeq; WP_012258865.1; NC_012032.1.
DR AlphaFoldDB; B9LBJ2; -.
DR SMR; B9LBJ2; -.
DR KEGG; chl:Chy400_3259; -.
DR HOGENOM; CLU_006301_5_1_0; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
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..745
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000202766"
FT DOMAIN 241..410
FT /note="tr-type G"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..257
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 275..279
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 296..299
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 350..353
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 386..388
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 7..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 250..257
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 296..300
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 350..353
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 745 AA; 79371 MW; CC891E5015FAFE70 CRC64;
MSDKPRRDTG STGTGSGRST GQSGSNRAVG APNPGTGRSP NASTGGNRSA GNQAGNSGRP
ASAGRNQATT PAPNRNTPPA GARQGGAANA RTGTPPVARG GGGGVTPPTG RGGNNPRAAR
NQPRSRQQPE EREREHVLRR PPPQPAARPV VRPRGPVALP PVMTVRELSE ATGIGAADIL
KAMLKAGMLA NINQQIDYET AALIMADFGI ETTEDVPEQM AGIVEDVKEV LRAQPPEEMR
PRPPVVTIMG HVDHGKTKLL DAIRSTRVAE GEAGGITQHI GAYQIEVNHR KITFLDTPGH
EAFTAMRARG AQVTDIVVLV VAADDGVKPQ TEEAIAHVKA AGVPMIVAIN KIDLPTANPD
RIKQQLANVG VIVEEYGGNV PCVHVSARQK INIDGLLEMI LLVADLEDLR ANPNAPAVGT
IIEAKLDKSR GPVATVLIQN GTLHLEDNVL VGCVAGKIKS MFSDSGKRLR HAEPSTPVEI
VGLEGVPQAG DILQVMDDLV VAREIALQRQ RQQRAEVMAA AARGTSLEEL FGKVKQGQVK
ELNLILKADV QGSLDAIAHL IEQLNQSQQA VQTRIIHRGV GAITEGDVNL ALASHAIIIG
FNARPDPAAR RHAEQHGIDI RFYNIIYQLQ DDLKKAMAGM LAPTVKEVVE GYAEVRNTFR
LPTREVVAGV YVSDGKITRT GQNVRVLRRG VVIHDGKISS LKRFKDDVRE VTAGYECGLI
VEGFNDIEVG DALEFYRQET VAASL
