IF2_LACJO
ID IF2_LACJO Reviewed; 880 AA.
AC Q74IS8;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=LJ_1487;
OS Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=257314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNCM I-1225 / La1 / NCC 533;
RX PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT "The genome sequence of the probiotic intestinal bacterium Lactobacillus
RT johnsonii NCC 533.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004).
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; AE017198; AAS09255.1; -; Genomic_DNA.
DR RefSeq; WP_004897131.1; NC_005362.1.
DR AlphaFoldDB; Q74IS8; -.
DR SMR; Q74IS8; -.
DR STRING; 257314.LJ_1487; -.
DR EnsemblBacteria; AAS09255; AAS09255; LJ_1487.
DR GeneID; 66435134; -.
DR KEGG; ljo:LJ_1487; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_0_9; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000000581; 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..880
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228206"
FT DOMAIN 381..550
FT /note="tr-type G"
FT REGION 34..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..397
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 415..419
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 436..439
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 490..493
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 526..528
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 47..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 390..397
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 436..440
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 490..493
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 880 AA; 98662 MW; FFEF5C758CCF7EB8 CRC64;
MAKKRIYEVA KELDIENKIV VKKAQDLGFD VKSHMSSLDD KQVSKLVDSL KSTNTTPSTE
KDSKNSSRKE KAKIKVSVGA IRRRDNKNEH DNRHGNNKHR NNNFKKQQNN RRENEDKKTT
SAKPAARDLL NKFKKKQRAE ASELNAQTEA SRRKWHQEQN PQRSKVKKVE NTRKPKEEKL
EGAAAVKARV QASQKPVGPK IIKPSPARNK AKRPTVKKVE PIAPVVPAPQ KEETKPTRKK
DFTRKKREVP DYERERSEHS DKARRRRNKK NKRINQSKEV KKQPTQRKER PLPETLVYEE
GMNAQDLGKL LHREPAEIVK KLFMLGVMTN QNQSLDKDTI ELLAAEYGIE AEEKVHEDIS
DIDTLYTKEM EESKASKHQE KRPPVVTIMG HVDHGKTTLL DRLRHTNVSE HEAGGITQRI
GAYQVRIDDR LITFLDTPGH AAFSNMRARG AEITDIVILV VAADDGVMPQ TIEAIDHAKS
AGVPIIVAVN KIDKPGANPD HVMEQLMKYG LVPEDWGGDT IFVKISAKTG KNVEELLQMI
LLQADVMELK ADPDQKAIGT VIEARLDKGR GSVADILVQQ GTLKVGDPIV VGDTFGRVRV
MTNDKGRRVK KATPSTPVEI TGLNDVPEAA DKLVVFDDEK TARSVGEQRA KNALEKQREN
VQHVTLDNLF DTMKKENMKE VDIVLKADVQ GSAEALQQSL EKIEVEGVRV NIIHSGVGAI
NESDVTLAGA SNAFIVGFNV RPTNTAKSQA DSEGVDIRLY NIIYKVMDDV EAAMKGMLEP
TYEEKVTGNL TVRETWKVSK IGTIAGAFVD NGYVTRDSGI RVIRDGIVKY DGKVASLKRF
KDDVKEVKQG FDCGITIENF NDIKVDDQLE AYEMQEVPVK
