IF2_LEUMM
ID IF2_LEUMM Reviewed; 834 AA.
AC Q03WH4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=LEUM_1355;
OS Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / DSM
OS 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523 / NBRC 100496 / NCIMB
OS 8023 / NCTC 12954 / NRRL B-1118 / 37Y).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=203120;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523
RC / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(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; CP000414; ABJ62448.1; -; Genomic_DNA.
DR RefSeq; WP_011680054.1; NC_008531.1.
DR AlphaFoldDB; Q03WH4; -.
DR SMR; Q03WH4; -.
DR STRING; 203120.LEUM_1355; -.
DR PRIDE; Q03WH4; -.
DR EnsemblBacteria; ABJ62448; ABJ62448; LEUM_1355.
DR GeneID; 61176166; -.
DR KEGG; lme:LEUM_1355; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_0_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 84734at2; -.
DR Proteomes; UP000000362; 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..834
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335488"
FT DOMAIN 335..504
FT /note="tr-type G"
FT REGION 1..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..351
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 369..373
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 390..393
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 444..447
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 480..482
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 43..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 344..351
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 390..394
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 444..447
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 834 AA; 90379 MW; 8EB81F784B599947 CRC64;
MTEEKKFSGS NRPARKQAVP ERKELPASQR RHAAKLADGT TPAQGGSRPS RPARPNNNNQ
NRPNNGGQSQ NRNNQNRSNT STGGQNRSNN GGNRNNRPGS RVAPAEGRPM IREKKNWSTK
PREGQVDYSA KPDNSLKQYV NENEKKRQAS AAAKHPKKPA AATKPAVKKE TSATKPATAS
TTTGAGKFGG ALASGNNSAR NNSRKRNTNG TGQQTPRRND RPRGSKKSRR IAAKHQPSTP
ATVRKEQPLP AVLEYRVGMN VQDLSKLLHR DTAEIIKKLF LLGIVTNQNQ SLDEDTIEIL
AADYGIEAQA KEEEDVADID RFFDDENIDE SKLVSRPPVV TIMGHVDHGK TTLLDYLRNS
HVTEGEAGGI TQHIGAYQTR INDKLITFLD TPGHAAFTEM RARGANVTDL TILVVAADDG
VMPQTIEAIN HAKAAGTPII VAVNKIDKPG ANPDDVMNQL MAYDLVPEEY GGDTIFVKIS
AKFGQNVDEL LEMILLQAEV LELKANPNMP ARGSVIEARL DKGRGPVSTV LVQQGTMHVG
DPIVVGNTYG RVRTMTNERG VELSEALPAT PIQITGLNGV PQAGDRFIVM ADEKTARAAG
EERAKRAQEA VRNSGSVVTL DTLFNTMAEK AMKTVPVIVK ADVQGSVEAL SGSLKKIEVD
GVRVDIIHTA VGAINESDVT LAEASGAIII GFNVRPTPLA KSQSDSEKVD IRFYNVIYNA
IDDVEAAMKG QLEPVYEEKV IGKVEVKELF KFSKVGTIAG AMVEEGKITK DSKVRVIRDN
VVVFDGEVGS LQRGKDAVNE VKMGFEFGFT VAKFNDVHAG DVVEAYVMEE VKPK
