IF2_LIMRD
ID IF2_LIMRD Reviewed; 752 AA.
AC A5VJE0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Lreu_0699;
OS Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=557436;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20016;
RX PubMed=21379339; DOI=10.1371/journal.pgen.1001314;
RA Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M.,
RA Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M.,
RA Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L., Ivanova N.,
RA Kyrpides N.C., Walter J.;
RT "The evolution of host specialization in the vertebrate gut symbiont
RT Lactobacillus reuteri.";
RL PLoS Genet. 7:E1001314-E1001314(2011).
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; CP000705; ABQ82964.1; -; Genomic_DNA.
DR RefSeq; WP_003668181.1; NZ_AZDD01000017.1.
DR AlphaFoldDB; A5VJE0; -.
DR SMR; A5VJE0; -.
DR STRING; 557436.Lreu_0699; -.
DR PRIDE; A5VJE0; -.
DR EnsemblBacteria; ABQ82964; ABQ82964; Lreu_0699.
DR GeneID; 66470840; -.
DR KEGG; lre:Lreu_0699; -.
DR PATRIC; fig|557436.17.peg.556; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001991; 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..752
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000057657"
FT DOMAIN 253..422
FT /note="tr-type G"
FT REGION 26..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..269
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 287..291
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 308..311
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 362..365
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 398..400
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 29..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..152
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 262..269
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 308..312
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 362..365
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 752 AA; 83538 MW; 0E2CE8B33AD44C0C CRC64;
MAKERIYELA KELKMPSKDL VNMANRQGMG VKSHMSSVTP DQAQQLRQLA KGGQKTTNNQ
HQPVKKNDGH NKQNNHQAQN HNQHHDHDKT QNERPQKKNN SRSNNGTKDN NQHQNNGGRF
GGSLNNDQGR NGKRFNKKNK KNKKHNKNKR LREVAHKQPT QRKDKPLPEV LEYTDGMNAQ
DLGKILHRSP AEIVKKLFML GVMINQNQSL DKDTIELLAT DYGIEAKEKV QVDVSDIDKM
FEDEQNNTEH QVTRPAVVTV MGHVDHGKTT LLDKLRHSHV TEHEAGGITQ EIGAYQVHYN
DQLITFLDTP GHAAFTEMRA RGANITDITV LVVAADDGVM PQTVEAIHHA QAAQTPIIVA
VNKIDKPGAN PDRVTEELAK YNLIPEDWGG DTIFVKISAK FGKNLDELLD MILLQAEMLE
LKANPDQNAA GSVVEARLDQ GRGSVATVLV QQGTLHVGDP IVVGNTFGRV RTMTNENGRR
IKEATPSTPV EITGLNEVPE AGDRFVVFDD EKTARAAGEE RAKRAMDKER QKTSHVTLDN
LFATMKKGQM KTLPIIIKAD VQGSVEALSQ SLQKIKVDGV RVDIIHQAVG AINQSDVTLA
EASNAVIIGF NVRPTAVAKT LADSNSIDIR LHRVIYDAIE EVEDAMKGML EPVYKEETIG
QVEVRQIYKA SKVGTIAGGM VTSGKITRDA KVRLVRDGVV IYEGELGSLK RFKDDVKEVK
QGYECGLTIE NYNDIKEMDV IEAYKMKEVP VK
