IF2_PELTS
ID IF2_PELTS Reviewed; 973 AA.
AC A5D2S0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=PTH_1269;
OS Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Pelotomaculum.
OX NCBI_TaxID=370438;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13744 / JCM 10971 / SI;
RX PubMed=18218977; DOI=10.1101/gr.7136508;
RA Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT evolution in anaerobic microbiota.";
RL Genome Res. 18:442-448(2008).
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; AP009389; BAF59450.1; -; Genomic_DNA.
DR AlphaFoldDB; A5D2S0; -.
DR SMR; A5D2S0; -.
DR STRING; 370438.PTH_1269; -.
DR PRIDE; A5D2S0; -.
DR EnsemblBacteria; BAF59450; BAF59450; PTH_1269.
DR KEGG; pth:PTH_1269; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3064; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR Proteomes; UP000006556; 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.
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..973
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000075611"
FT DOMAIN 472..641
FT /note="tr-type G"
FT REGION 52..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..488
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 506..510
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 527..530
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 581..584
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 617..619
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 79..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 481..488
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 527..531
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 581..584
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 973 AA; 107814 MW; 73E3D0E07B2F3DE8 CRC64;
MVKKRVHELA KELKIESKEI INRLNQMGIN VKSHMSTLED GVVERLHQLY RPDQEEVKPA
AAKPPAAGQT IKPEEVAPQA QPESRKKDAA MLDSQKPDRD RVQKNGRERA GKATRADHYK
GAGLVERVPS RPPDRRFQER PKQSDKARPW GQPRADQGAR LKTADFVQER TRSARAGQDY
SQPEKVQQER VQDRQQKERP PFEKAQQPRP QHEHKPQDSV KERPHPERAS READNAKRAE
RLDKGAGKTA EIAYKSGLKA LEKAQVGTKP QRAGERGARP GGLHETKPKK NLAPGDAGYA
KLWQEQTPVI PQKLLDDRRR QTEEKVKVTE KQKQQAKSQK LVKSREKRNA MAELAEERLR
PRPAVAGSRK KGAAKPQEQA QKPAQPLEKK PIVLGESTTV QELALKMHKS PAELIKKLMQ
LGVMATINQE IDTDTATILA GEFGYEVEVK LPVDIEAMLM QEPEDDPVSL QDRPCVVTVM
GHVDHGKTSL LDAIRETNVT ATEAGGITQH IGAYQVEHNG KKITFLDTPG HEAFTAMRAR
GARVTDIAIL VVAADDGVMP QTVEAINHAK EAKVPIIVAI NKIDKPGANP DRVKQQLTEH
GLVAEEWGGD TICVNVSALK KEGLKDLLEM ILLVAEMSEL KANPNRPARG TVIEAELDKG
RGPVANVLVQ NGTLNVGDTL IAGAAFGRVR AMMDDKGRRI KKAGPSTPVE VLGFSEVPQA
GDIFVVVEDE KLARTIVARR QARKREEELK STARVSLADL FKHIQEGQIK ELGIIIKADV
QGSVEALRQA LERLSTDEVR VNIIHGGVGA ITETDVMLAS ASNAIIIGFN VRPDVNARKA
AENEKVDVRL YRVIYDAIED VKAAMSGLLE PEYREVTLGR AEIRKIFRSS KIGNIAGCYV
LEGKIERDAS VRVIRDGIVV HEGKLESLKR FKDDVREVVQ GYECGIALEK FNEIQEGDII
EAFTVEAIKR QLT
