IF2_LATSS
ID IF2_LATSS Reviewed; 937 AA.
AC Q38W81;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=LCA_1248;
OS Latilactobacillus sakei subsp. sakei (strain 23K) (Lactobacillus sakei
OS subsp. sakei).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Latilactobacillus.
OX NCBI_TaxID=314315;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=23K;
RX PubMed=16273110; DOI=10.1038/nbt1160;
RA Chaillou S., Champomier-Verges M.-C., Cornet M., Crutz-Le Coq A.-M.,
RA Dudez A.-M., Martin V., Beaufils S., Darbon-Rongere E., Bossy R., Loux V.,
RA Zagorec M.;
RT "The complete genome sequence of the meat-borne lactic acid bacterium
RT Lactobacillus sakei 23K.";
RL Nat. Biotechnol. 23:1527-1533(2005).
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; CR936503; CAI55552.1; -; Genomic_DNA.
DR RefSeq; WP_011374945.1; NC_007576.1.
DR AlphaFoldDB; Q38W81; -.
DR SMR; Q38W81; -.
DR STRING; 314315.LCA_1248; -.
DR EnsemblBacteria; CAI55552; CAI55552; LCA_1248.
DR KEGG; lsa:LCA_1248; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_0_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 90456at2; -.
DR BioCyc; LSAK314315:LCA_RS06205-MON; -.
DR Proteomes; UP000002707; 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..937
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228207"
FT DOMAIN 438..607
FT /note="tr-type G"
FT REGION 47..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..454
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 472..476
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 493..496
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 547..550
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 583..585
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 72..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 447..454
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 493..497
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 547..550
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 937 AA; 103216 MW; 5FC72EF331C4B31C CRC64;
MGKKRIYELA KEINVASKDI LETANKKGYD LKNHMATIDD NQEKTLRAAF QTKATPAASK
PATPAAPKAS EKSESGKIKI NKTAIRRRPE ADKKPAQHSN NRPQANANRN GQASNGQNRT
NNARPNNNSA RPNNSRPNTN SRPNNNSQNR STSANHPMSL QEQISQANAR RQRTQERIQQ
QREQREADEK KRREQANRPR PTRNNASNNR PSNGKPTNGA RPTTNSPRPT VTKDGRPLGS
SRPNNNNSAR PNTTNNRPTN SRPATTPSRP VSAQEMQQKM QANTVSASKP ASNNTASKPK
NFGPDKKRGG GYNSYGNSQQ RFNKKRKKTR KQQLAEQNAA KKEMPQRKER PLPEVLVFSE
GMNVADIAKK IHREPAEIIK KLFMLGIMVN MNQSLDKDTI ELLATDYGIE AEQKVEVDIA
DIDSVFETEA KSDANLVSRP PVVTIMGHVD HGKTTLLDNL RNSHVTDGEA GGITQHIGAY
QTKLNDRLIT FLDTPGHAAF TNMRARGADI TDIIILVVAA DDGVMPQTIE AINHAKAAKA
PIIVAVNKID KPGANPDHVM EQLMGYGLVP EDWGGDTIFV KISAKTGENI DDLLEMVLLE
ADVLELKANR DQKAVGTVIE ARLDKGKGPV ASLLVQQGTL RIGDPIVVGN TFGRVRVMTN
DRGRRVKEVF PSEPVEITGL NDVPQAADRF VVFEDEKTAR AAGEERAKRA LLKERSRSNP
VTLDNLFETM KQGELKEVGV IIKADVQGST EALAGSLRKI EVEGVRVNII HEAVGAINES
DVTLAAASNA IIIGFNVRPT PQAKIQADAE QVDIRLHRII YKAIEEIEAA MKGMLEPVYE
EKVTGQLTVR ETYNVSKIGT IAGCIVDTGV IRRDSGVRLI RDSIVIYEGK LSSLKRFKDD
VKEVKTGFEC GVTIEDYNDI KIDDQIEAYV MEEVPVK
