IF2_NATTJ
ID IF2_NATTJ Reviewed; 673 AA.
AC B2A397;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Nther_1444;
OS Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 /
OS JW/NM-WN-LF).
OC Bacteria; Firmicutes; Clostridia; Natranaerobiales; Natranaerobiaceae;
OC Natranaerobius.
OX NCBI_TaxID=457570;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.;
RT "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN-
RT LF.";
RL Submitted (APR-2008) 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; CP001034; ACB85027.1; -; Genomic_DNA.
DR RefSeq; WP_012447901.1; NC_010718.1.
DR AlphaFoldDB; B2A397; -.
DR SMR; B2A397; -.
DR STRING; 457570.Nther_1444; -.
DR EnsemblBacteria; ACB85027; ACB85027; Nther_1444.
DR KEGG; nth:Nther_1444; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001683; 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; 2.
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; Reference proteome.
FT CHAIN 1..673
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093806"
FT DOMAIN 171..340
FT /note="tr-type G"
FT REGION 32..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..187
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 205..209
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 226..229
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 280..283
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 316..318
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 35..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 180..187
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 226..230
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 280..283
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 673 AA; 74857 MW; 79A93DBFA0C50D04 CRC64;
MEKIRVYQLA KEIGLESKEL VTTLQELDIS VKNHMSTLSE EEADTVRELY TESSAKDEDN
KDETSQQQDE KQEDKKEQGT TTDKPLVAPP ITVGELAEQI GVESTSIITK LISKGVMANI
NQNLEEDSLE YLAQEFDFVV TQEEPEEDEK SEEDRIIEQI RSEEPKGEPL ERAPVVTVMG
HVDHGKTSIL DSIRKTKSIE KEAGGITQHI GASRVLYNDK TVVFLDTPGH EAFTEMRARG
AHVTDIAILV VAADDGVMPQ TVEAINHAKS AGVPIIVAIN KTDKPDANPD RVKQELTEYN
LVTEEWGGDT ICVSVSAVQN EGIDELLEMV QLVAEMNELT SYPQNTGKGT VIEAKLDKGR
GPVATVLVED GTLKVGDSVL CGSTFGNIRA MVDDRGKRLK QANPVTPVEI LGLENIPEAG
DEFQVVPDEK MAREIAKKKQ EKEREEKLKR SQSVSLDNLF DQIKEGEQKE LNIIVKGDVR
GSVEALRESL LKLNDNEHEI KVNVIHAGVG TVSESDIMLA VASNAIIIGF NVRPDPNARK
AAEREQIDMR VYRVIYEAIE DVKAAMAGLL DPEYKEVVQG QIEVRQLFKV SRIGTIAGCY
VTDGYIRNNS YIRVIRDGRV IHEGNIKNLK RFQDDVKEVQ QGYECGILLE KFNDLKEGDI
FEAYTYEEIS PDV
