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IF2_LACCB
ID   IF2_LACCB               Reviewed;         943 AA.
AC   B3WER5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=LCABL_17860;
OS   Lacticaseibacillus casei (strain BL23) (Lactobacillus casei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=543734;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL23;
RA   Maze A., Boel G., Bourand A., Loux V., Gibrat J.F., Zuniga M., Hartke A.,
RA   Deutscher J.;
RT   "Lactobacillus casei BL23 complete genome sequence.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; FM177140; CAQ66866.1; -; Genomic_DNA.
DR   RefSeq; WP_012491636.1; NC_010999.1.
DR   AlphaFoldDB; B3WER5; -.
DR   SMR; B3WER5; -.
DR   PRIDE; B3WER5; -.
DR   KEGG; lcb:LCABL_17860; -.
DR   HOGENOM; CLU_006301_5_0_9; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 69576at2; -.
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.
FT   CHAIN           1..943
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000093796"
FT   DOMAIN          444..613
FT                   /note="tr-type G"
FT   REGION          46..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          453..460
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          478..482
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          499..502
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          553..556
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          589..591
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        54..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..205
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..284
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..329
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..359
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         453..460
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         499..503
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         553..556
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   943 AA;  103151 MW;  01B5958EAC6C5C54 CRC64;
     MGKKRVYEFA KEMHVDNKDV IDIAKNLGIE VKNHMSSIDQ DQEAKIKGML SKQSAGKAPS
     SQAAKTPAKA AKTSSAAHKE AAKKPVAASA KSNDHADVAE HSQKNAKPAA KQENKPARSN
     KTSDGKIILS KSTILRPRST QTAHTNTNHN RGGNTASANN TANGRNSNRS NNNNNNRSAN
     NANRSGNNNR SNERNRNDRN RRFDNQRVTG PMPRAGRPTA ANGNPRPVAG NGGKFVKPAS
     ERQQPKRQEA VKPANAASKR SEQPRTERPR TEQPAATTNQ RFTKPAPVPA AAAPKPASAG
     SQDNRNSRRG GGNSNFGRSN SYGNRNGFNR NNRRNKKNKR RQQSAPKKEM PQRKERPLPE
     TLIYEVGMNA QDLGKILHRE PAELIKKLFM LGVMVNQNQS LDKDTIELLA TDYGIDAQEK
     VHEDISDLDK VFEEENKNQD NLQPRPPVVT IMGHVDHGKT TLLDKLRHTH VTEGEAGGIT
     QHIGAYQVKL RDRLITFLDT PGHAAFTNMR ARGADITDIV VLVVAADDGV MPQTIEAIHH
     AQAAKAPIIV AVNKIDKPGA NPDHVMEQLT EYGLIPEDWG GDTIFVKISA KFGKNIDELL
     EMILLEADVL ELKANPDQKA VGTVIEARLD KGKGPVATVL VQQGTLHTGD PIVVGNTFGR
     VRAMTNDHGR RVKDALPSMP VEITGINDVP QSADKFVVFA DERTARAAGE ERAKRAQEEE
     RKNTNHVTLD NLFETMKEGQ LKEVDVIIKA DVQGSVEALA GSLEKIEVKG VRVNIIHQAV
     GAINESDVTL AAASNAIIIG FNVRPTALAK AQAEQDDVDI RLHSVIYKAI EEVEAAMKGM
     LEPTYEEKVI GTVTVRETIP VSKVGTVVGG YVDSGYITRD AGVRLVRDGI VKYEGKLGSL
     RRFKDDVKEV RQGFELGLTI ENYNDIKVDD QIEAFTMEQV PVK
 
 
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