ID   IF2_ENTFC               Reviewed;         784 AA.
AC   P18311;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Translation initiation factor IF-2;
GN   Name=infB;
OS   Enterococcus faecium (Streptococcus faecium).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1352;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3063954; DOI=10.1007/bf00330501;
RA   Friedrich K., Brombach M., Pon C.L.;
RT   "Identification, cloning and sequence of the Streptococcus faecium infB
RT   (translational initiation factor IF2) gene.";
RL   Mol. Gen. Genet. 214:595-600(1988).
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.
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; M36878; AAA26900.1; -; Genomic_DNA.
DR   AlphaFoldDB; P18311; -.
DR   SMR; P18311; -.
DR   STRING; 1352.AL014_07465; -.
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.
FT   CHAIN           1..784
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000137203"
FT   DOMAIN          285..454
FT                   /note="tr-type G"
FT   REGION          31..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..301
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          319..323
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          340..343
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          394..397
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          430..432
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        52..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         294..301
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         340..344
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         394..397
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   784 AA;  86302 MW;  7F7B63779D4DA434 CRC64;
     MSNKRIYELA KELNQPSKDV VEKAQQLGIN VKNHMGTITT GDEKKLQQAF KKPQTNKKPA
     QQASQKPATN QPNEQKKQET KTKQQKNNRN YQDRGQGSGQ VNQGKNQSTN QNRSNNGGGN
     NQNRQGATQS GNQNRQGSTQ GGNQNRQGSN QGGNQNRNNN NNRGKFNNNN RNRFNKKGKK
     GKQQTSNKPA VPPRKFRELP EVLEYTEGMN VADIAKKIHR EPAEIIKKLF MLGVMVNQNQ
     ALDKDTIELL ATDYGMEPQE KIQVDIADID KFFEPEELNP DTLVSRPPVV TIMGHVDHGK
     TTLLDTLRHS RVTSGEAGGI TQHIGAYQID IDGKPITFLD TPGHAAFTSM RARGASITDI
     TILVVAADDG VMPQTVEAIN HAKAAGVPII VAVNKIDKPG ANPQHVMQEL SEYELIPEAW
     GGETIFVEIS AKFGQNIDEL LEMILLVAEV EDLKADPKQR AIGTVIEARL DKGKGPVTTL
     LVQQGTLNVG DPIVVGNTYG RVRVMVNDLG RREKSAGPAT PVEITGLNDV PQAGDRFVVF
     EDEKTARAAG EERAKRALLE HRAITSRVTL DNLFESLKEG ELKEVNVIIK ADVQGSAEAL
     AASLQKIDVE GVRVKIVHSA VGAINESDVT LAAASNAIII GFNVRPTPQA KIQADNEEVD
     IRLHRIIYKA IEEIETAMKG MLDPEFEEKI TGQMIVRETF KVSKVGTIAG AYVTEGYIRR
     DSGVRVIRDG IVIYEGQLAS LKRFKDDVKE VKMGYECGAM IEKFNDIKVD DVIEGFIMEE
     IKTN