IF2_LIGS1
ID IF2_LIGS1 Reviewed; 737 AA.
AC Q1WUF4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=LSL_0572;
OS Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=362948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCC118;
RX PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT "Multireplicon genome architecture of Lactobacillus salivarius.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006).
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; CP000233; ABD99381.1; -; Genomic_DNA.
DR RefSeq; WP_011475823.1; NC_007929.1.
DR RefSeq; YP_535464.1; NC_007929.1.
DR AlphaFoldDB; Q1WUF4; -.
DR SMR; Q1WUF4; -.
DR STRING; 362948.LSL_0572; -.
DR PRIDE; Q1WUF4; -.
DR EnsemblBacteria; ABD99381; ABD99381; LSL_0572.
DR KEGG; lsl:LSL_0572; -.
DR PATRIC; fig|362948.14.peg.651; -.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000006559; 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..737
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008262"
FT DOMAIN 238..407
FT /note="tr-type G"
FT REGION 55..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..254
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 272..276
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 293..296
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 347..350
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 383..385
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 55..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..134
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 247..254
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 293..297
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 347..350
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 737 AA; 82194 MW; ED10151360DA7041 CRC64;
MVKKRIYELA KELGISSERV IEIAKKYDFK VTNHMSALDE NEQNKIRGSI SLKAKKKEHI
QHNKNKDNFH SKKVQKSNTG SKDENNHKNV HKNNRKRSGS SMKENNNAKN GQRNNRNNRS
NNKFKNKRNN NNKRNNNFKK GNPVPPRKNK PLPETLVYTV GMNVADIAKK IHREPAEIIK
KLFMMGVMVN QNQSLDKDTI ELLAADYGIN AEEKVEVDVS DIDKFFEEEQ NNTEHLEKRP
PVVTIMGHVD HGKTTLLDKL RHTHVTEGEA GGITQHIGAY QVRHDDKIIT FLDTPGHAAF
TNMRARGADI TDITVLVVAA DDGVMPQTIE AINHAKAAGV PIIVAVNKID KPGANPNHVM
EQLTEYELIP ESWGGDTIFV EISAKFGKNL DELLDMILLE AEMLELHANP NQRGAGSVIE
ARLDKGKGSV ASLLVQQGTL HVGDPIVVGN TFGRVRTMVD ARGYDIKKAT PATPVEITGL
NEVPDSGDRF ITFEDEKTAR AAGEKRAERA LLKERSQTNH VTLDNLFDTL KEGELKEVGV
IIKADVQGSV EALAQSFKKI DVEGVRVNII HQAVGAINES DVTLAEASNA IIVGFNVRPT
PLAKQQAESD NVDIRLHRVI YKAIDEIETA MKGMLEPEYQ EKITGQVEIR QTYKVSKLGT
IGGGYVIDGY IRRDSGVRVI RDGIVIYEGK LASLKRFKDD VKEVKQGYEC GLMIEKYNDI
KVGDQIEAYI MEEVPVD
