IF2_LEUCK
ID IF2_LEUCK Reviewed; 840 AA.
AC B1MZH4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=LCK_01099;
OS Leuconostoc citreum (strain KM20).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=349519;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KM20;
RX PubMed=18281406; DOI=10.1128/jb.01862-07;
RA Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., Kim J.-S.,
RA Lee S., Park H.-S., Park Y.-H., Oh T.K.;
RT "Complete genome sequence of Leuconostoc citreum KM20.";
RL J. Bacteriol. 190:3093-3094(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; DQ489736; ACA82926.1; -; Genomic_DNA.
DR RefSeq; WP_004904724.1; NC_010471.1.
DR AlphaFoldDB; B1MZH4; -.
DR SMR; B1MZH4; -.
DR STRING; 349519.LCK_01099; -.
DR PRIDE; B1MZH4; -.
DR EnsemblBacteria; ACA82926; ACA82926; LCK_01099.
DR KEGG; lci:LCK_01099; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_0_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 84734at2; -.
DR Proteomes; UP000002166; 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; 1.
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.
FT CHAIN 1..840
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335487"
FT DOMAIN 341..510
FT /note="tr-type G"
FT REGION 1..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..357
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 375..379
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 396..399
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 450..453
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 486..488
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 350..357
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 396..400
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 450..453
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 840 AA; 91145 MW; 89BBC73C6AEA4ACB CRC64;
MTEEKKFSSS NRPARKQAVP ERKELPASQR RHAAKLTDGT NSSAGTTPRS NKPARQGQSQ
GQGQNRHTNS SRSNTQGGNA SRPNQSKSQG QGGRNNQRPG SRTQASEGRP MIREKKNWST
KPREGQIDYS KKTDNSLKQY VSENEKRKQA AAAKTTKKPA EQSKKAAEKP AQTKPKTAET
KTTATTTQSG TGKFGGALAS GNNSARNNSR KRNTNGTGQQ TPRRNDKPRG SKKSRRIAAK
KGPAVPATER KEQPLPAVLE YRIGMNVQDL SKLLHRDTAE IIKKLFLLGI VTNQNQSLDA
DTIEILAADY GIESQLKEEE DVADIDKFFE DDTIDESKLV ARPPVVTIMG HVDHGKTTLL
DYLRNSNVTE GEAGGITQHI GAYQTQLNGK TITFLDTPGH AAFTEMRARG ANVTDLTILV
VAADDGVMPQ TIEAINHAKA AETPIIVAVN KIDKPGANPD EVMNQLMAYD LVPEEYGGDT
IFVKISAKFG QNVDELLEMI LLQAEVLELK ANPDVPARGS VIEARLDKGR GPVATVLVQQ
GTMRVGDPIV VGNTYGRVRT MTNERGIELA EALPATPVQI TGINEVPQAG DRFIVMADEK
TARAAGEERA KRAQEAIRNS GSVVTLDTLF STMSEKAMKT VPVIVKADVQ GSVEALSGSL
KKIEVDGVRV DIIHTAVGAI NESDVTLASA SGAIIIGFNV RSTPLAKSQA DSDKVDIRFY
NVIYNAIDDV EAAMKGQLEP VFEEKVIGNV TVKELFKFSK VGIIAGAMVE EGKITKDSKV
RIMRDNVVVY DGEVASLQRG KDSVNEVKMG YEFGFTVAKY NDIRVGDTVE AYIMEEVKVK
