IF2_LACH4
ID IF2_LACH4 Reviewed; 870 AA.
AC A8YVQ7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=lhv_1342;
OS Lactobacillus helveticus (strain DPC 4571).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=405566;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DPC 4571;
RX PubMed=17993529; DOI=10.1128/jb.01295-07;
RA Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K.,
RA McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F.,
RA Beresford T., Ross R.P.;
RT "Genome sequence of Lactobacillus helveticus: an organism distinguished by
RT selective gene loss and IS element expansion.";
RL J. Bacteriol. 190:727-735(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; CP000517; ABX27344.1; -; Genomic_DNA.
DR RefSeq; WP_012212000.1; NC_010080.1.
DR AlphaFoldDB; A8YVQ7; -.
DR SMR; A8YVQ7; -.
DR STRING; 405566.lhv_1342; -.
DR PRIDE; A8YVQ7; -.
DR EnsemblBacteria; ABX27344; ABX27344; lhv_1342.
DR KEGG; lhe:lhv_1342; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_0_9; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000000790; 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.
FT CHAIN 1..870
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000071290"
FT DOMAIN 371..540
FT /note="tr-type G"
FT REGION 49..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..387
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 405..409
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 426..429
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 480..483
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 516..518
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 49..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..271
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 380..387
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 426..430
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 480..483
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 870 AA; 97279 MW; 0BF4BC996F8E39DD CRC64;
MAKKRIYEVA KEVGVDNKVV VQKAKELGFD VKNHMSSIDD AQVAKLKGSF QNSAPAEKNN
KIKISVSSIR KNEKKQEDNA GSKKPRRRNN KRLQNNDRNH KNRNDRDHSA NSGSGKPKAA
ALLQQFKQKQ RAEEGQLNRQ AQKAKKEYHE QLKYPKKEQP VNNKKKTNKE SNNKKSEEVE
KKVIGPKILK PSPARLKKNQ PSTNEKPAVK VSIPEPPKEE KRNNGRGKNM GKPGHKGKNQ
FFNNHSEQSD RSERKRRKNK NKKRKQEQKP KKQITKRKER PLPETLVYEK GMNAQDIGKL
IHREPAEIVK KLFMLGVMTN QNRSLDKDTI ELLAAEYGIN AKQKVHEDIS DIDTLYNKRM
EASKKSKNQV KRPPVVTIMG HVDHGKTTLL DRLRHTHVSA HEAGGITQKI GAYQVRLDDR
LITFLDTPGH AAFSNMRARG AEITDIVVLV VAADDGVMPQ TVEAIDHAKS ANVPIIVAIN
KMDKPGANPQ HVTEELMKYN LIPEDYGGDT IFVNISARTG QNVDDLLQMI LLQADMMELK
ANPTEMAIGT VIEARLSRGR GPVADVLIQQ GTLNIGDPIV VGDTFGRVRT MTNDRGRQVK
KATPSEPVEI TGLNDVPESA DKLVEFKDEK TARSVGEARA QQALQKSREN VQHVTLDNLF
DTMKKENMKE VDIVLKADVQ GSVEALQQSL EKIEVEGVRV NIIHSGVGAI NESDVTLAGA
SNAFIIGFNV RPTATAKSQA ETEGVDIRLY SIIYKAIDDV TAAMKGMLEP TYEEKVIGNL
TVRETWKVSK VGTIAGSFVD KGLVKSDAKI RIIRDGIVKY DGEIASLKRF KDDVKEVKQG
NDCGLTIKDY NDIKVGDEFE VYEMQQVEPK
