IF2_LACPL
ID IF2_LACPL Reviewed; 858 AA.
AC Q88VK7; F9UPZ7;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=lp_2040;
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
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; AL935263; CCC79286.1; -; Genomic_DNA.
DR RefSeq; WP_011101641.1; NC_004567.2.
DR RefSeq; YP_004889800.1; NC_004567.2.
DR AlphaFoldDB; Q88VK7; -.
DR SMR; Q88VK7; -.
DR STRING; 220668.lp_2040; -.
DR EnsemblBacteria; CCC79286; CCC79286; lp_2040.
DR KEGG; lpl:lp_2040; -.
DR PATRIC; fig|220668.9.peg.1725; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_0_9; -.
DR OMA; NRDNRTG; -.
DR PhylomeDB; Q88VK7; -.
DR BioCyc; LPLA220668:G1GW0-1747-MON; -.
DR Proteomes; UP000000432; 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..858
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137213"
FT DOMAIN 359..528
FT /note="tr-type G"
FT REGION 49..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..375
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 393..397
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 414..417
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 468..471
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 504..506
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 49..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 368..375
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 414..418
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 468..471
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 858 AA; 93662 MW; 27EC1625CC380891 CRC64;
MGKKRIYELA KELNVPSKQL IAQAQQLGFS VKNHMSTLGD SEARQLQGTT TVTHPKSQPA
PAKTSRATQA VAKNVTRTAN QQQSNSRHQQ SGDYLNNNRN NNQNNSQSRN SNGNRSNNGG
NRTNSNNGNR SANASRSNSA RNNGGSNTNR SNNNNNNNRS NNNNRSNTSN NRTNSTGNRT
NNGGQNRNNN RTTTNNNNNN SNRSNGSNNS SRNGSGRFGG SLNSNNNGGG RYRGGNNNNR
RRNNRNNKSR NNKNQRIRQV NNKPAPVRKD KPLPETLVYT VGMNAQDLGK LLHREPAEII
KKLFMLGVAV NQNQSLDKDT IEILATDYGI NAQEKVQVDV TDLDKFFDDE VNNTDNLAPR
APVVTVMGHV DHGKTTLLDQ LRHTHVTEGE AGGITQAIGA YQVKHDGKVI TFLDTPGHAA
FTEMRARGAD ITDITVLVVA ADDGVMPQTI EAINHAKAAK VPIIVAVNKI DKPGANPNHV
MEQLTEYGLI PEDWGGDTIF VQISAKFGKN LDELLDMILL QSEVLELTAN PKQNAAGSVL
EASLDRGKGS TATLLVQQGT MHVGDPIVVG NTYGKVRTMT NDHGKRIKEA VPSTPIEITG
LNDVPDAGDR FVVFDDEKTA RDAGEQRAKQ ALMEERKQTA HVTLDNLFDS MKQGELKEVD
VIIKADVQGS VEALAGSLRK IDVEGVRVNI IHTAVGAINE SDVALAEASN AIIIGFNVRP
TPQAKAQADT DDVDIRLHQV IYNAIDEIES AMKGMLEPTY KEEITGQAEI REIYKVSKIG
TIGGGMVTDG VIHRDSGVRV IRDGVVIYDG KLASLRRFKD DVKEVKQGFE LGLRIEDYND
IKVNDVIEAY VMKEVPVE
