IF2_LACLA
ID IF2_LACLA Reviewed; 944 AA.
AC P58002; Q9CHG4;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB; OrderedLocusNames=LL0767; ORFNames=L0372;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE005176; AAK04865.1; -; Genomic_DNA.
DR PIR; G86720; G86720.
DR RefSeq; NP_266923.1; NC_002662.1.
DR RefSeq; WP_003132492.1; NC_002662.1.
DR AlphaFoldDB; P58002; -.
DR SMR; P58002; -.
DR STRING; 272623.L0372; -.
DR PaxDb; P58002; -.
DR PRIDE; P58002; -.
DR EnsemblBacteria; AAK04865; AAK04865; L0372.
DR KEGG; lla:L0372; -.
DR PATRIC; fig|272623.7.peg.822; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_0_9; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000002196; 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..944
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137211"
FT DOMAIN 443..614
FT /note="tr-type G"
FT REGION 50..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..459
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 477..481
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 498..501
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 552..555
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 590..592
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 61..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 452..459
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 498..502
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 552..555
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 944 AA; 103710 MW; EC752207A15148E6 CRC64;
MSDKKRINQI AKETGLTNAE LVSAAQTLGF EVKSHSSSVT AEQAEKIIQS AKTGTDQTAK
VAEKPVKKSQ PKAAESAKKN KEDHPRTFAG KAVVEDPAIL ARIKAKEEAE KAAKVEVAST
EHPVVTEKPK ASEPVKKAEP KVEAKSEPKV EKVETKDNTA TSKAEVKPEN VADKKEPVVT
EEKKKSLTQK PRIQIKVIKR AEDIKKEQAA ARPEKKKFDK NRNDRNNRSD NRRPNQNGNG
QGGNHYDKNR SSGQGQNQGQ KRDKFASSGS APATDSFTPA TSGKTSRRDR DRKKSDNNRD
NTKDGNRKGG PLRVNDNRNQ VRNARNSNWN QKGGRGRYQN NQSSSVPATQ RKFHELPESL
EYEVGMNVQD IAKSIKREPA EIIKKLFMMG TMVNQNQSLD EDTIELILMD YGVTPVKKVE
EDKSDIERLF VEDGYLKEEN MVERPAVVTI MGHVDHGKTT LLDRFRESRV TEGEAGGITQ
HIGAYQIKAN GKKITFLDTP GHEAFTSMRA RGASVTDITI LVVAADDGVM PQTIEAINHS
KAAGVPIIVA INKIDKPGAN PQRVTQELTE HGVFPVAWDP ENGSEFVEIS AKFNQNLDEL
LDTVLLVAEV QELKADPTVR AIGTVVEARL DQGKGAIATL LVQQGTLHVQ DPIVVGNTYG
RVRTMTNDLG RRIKEAGPST PIELTGLSDV PQAGDHFAVF EDEKAARAAG EERAKRAQLI
KRQNTRRVNL DNLFDTLKEG QTKSVNIIIK ADVQGSAEAL AASLQKIEVE GVKVDIVHSA
VGAISESDIS LAAASNAIII GFNVRPTGLA REQAAQEEVD IRLHSIIYKV IEEVETAMRG
MLDPEFKEEI IGEAIVRETF NVSKVGTIAG FMVIRGKVAR DASVRVIREG VVIHDGAIAS
LKHFKDDVKE VGNAQEGGLM VEDFNDVEID DTFEVYKMVE IERK
