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 27-MAR-2024, entry version 84.
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; Bacillota; 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 AlphaFoldDB; B3WER5; -.
DR SMR; B3WER5; -.
DR KEGG; lcb:LCABL_17860; -.
DR HOGENOM; CLU_006301_5_0_9; -.
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; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 1.10.10.2480; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
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
//
