ID   IF2_LISMH               Reviewed;         781 AA.
AC   B8DG02;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=LMHCC_1245;
OS   Listeria monocytogenes serotype 4a (strain HCC23).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=552536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HCC23;
RX   PubMed=21602330; DOI=10.1128/jb.05236-11;
RA   Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., Bridges S.M.,
RA   Lawrence M.L.;
RT   "Genome sequence of lineage III Listeria monocytogenes strain HCC23.";
RL   J. Bacteriol. 193:3679-3680(2011).
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; CP001175; ACK39592.1; -; Genomic_DNA.
DR   RefSeq; WP_012581383.1; NC_011660.1.
DR   AlphaFoldDB; B8DG02; -.
DR   SMR; B8DG02; -.
DR   KEGG; lmh:LMHCC_1245; -.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   OMA; NRDNRTG; -.
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..781
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000118765"
FT   DOMAIN          282..451
FT                   /note="tr-type G"
FT   REGION          44..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..298
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          316..320
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          337..340
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          391..394
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          427..429
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        64..167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         291..298
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         337..341
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         391..394
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   781 AA;  84810 MW;  C5BDAAB429F68CC8 CRC64;
     MSKVRVYEYA KEHQVSSKKV IEALKDLGIE VANHMSTINE NALRQLDNAV DGTNKKAEAP
     KKETTSNENG NSKGPNKPNM TNSNEKSNKP NKPAGQANKP ATANKSQGAK PATNKPANTG
     NQTQASGNQQ AGGQKRNNNN NSNRPGGGNP NRPGGNNRPN RGGNFNNKGR NTKKKGKLNH
     STVPPTPPKP KELPEKIVFS ESLTVAELAK KLYREPSELI KKLFMLGVVA TINQSLDKDA
     IELICDDYGV QVEEEIKVDV TDLDVYFENE LNEAVDESKL VERPPVVTIM GHVDHGKTTL
     LDSLRNTKVT LGEAGGITQH IGAYQLEIHN KKITFLDTPG HAAFTAMRAR GAQITDITIL
     VVAADDGVMP QTIEAINHAK AAGMPIIVAV NKIDKPQANP DRVMQELTEY ELVPEAWGGD
     TIFAPISAKF GEGLENLLDM ILLVSEVEEL KANPDRRAIG SVIEAELDKG RGPVATLLVQ
     DGTLNIGDPI VVGNTFGRVR AMVNDLGRRV KKVGPSTPVE ITGLNDVPQA GDRFVVFEDE
     KTARNIGETR ASRALVAQRS ATNRVSLDNL FEHMKAGEMK EVNVIIKADV QGSVEALAAS
     LRKIDVEGVN VKIIHTAVGA INESDITLAA ASNAIIIGFN VRPTTQAREA AENESVDIRL
     HRVIYKAIDE IEAAMKGMLD PEFQEKIIGQ AQVRQTINVS KVGTIAGCYV TDGKITRDSG
     VRIIRDGIVV FEGEIATLKR FKDDAKEVAK GYECGITVQN FNDIKEDDVI EAYVMEEIER
     K