ID   IF2_MACCJ               Reviewed;         726 AA.
AC   B9EBE9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=MCCL_0853;
OS   Macrococcus caseolyticus (strain JCSC5402).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX   NCBI_TaxID=458233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC5402;
RX   PubMed=19074389; DOI=10.1128/jb.01058-08;
RA   Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT   "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT   reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL   J. Bacteriol. 191:1180-1190(2009).
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; AP009484; BAH17560.1; -; Genomic_DNA.
DR   RefSeq; WP_012656760.1; NC_011999.1.
DR   AlphaFoldDB; B9EBE9; -.
DR   SMR; B9EBE9; -.
DR   STRING; 458233.MCCL_0853; -.
DR   PRIDE; B9EBE9; -.
DR   EnsemblBacteria; BAH17560; BAH17560; MCCL_0853.
DR   KEGG; mcl:MCCL_0853; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_9; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000001383; 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..726
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000118766"
FT   DOMAIN          227..396
FT                   /note="tr-type G"
FT   REGION          50..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..243
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          261..265
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          282..285
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          336..339
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          372..374
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        50..91
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         236..243
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         282..286
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         336..339
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   726 AA;  79857 MW;  D57C471D4AE62D6A CRC64;
     MSKKRIYEYA KEVSLKSKDI IDALKKMNIE ASSHMQVIEA KEIAALDKIF KKSDTKSEVK
     SEQKAEAKKE EPNKEQPKKE EPKKQSDQKR PQNNNQKRNP NHRPGSHNKP GTGGPSKNKK
     GKGKGKQKPE PKQEVPVVKE TPSKITYEEG ITVGELAEKL GKDASEIVKN LFMVGIMANI
     NQSLNQEAIE LICDEYGVEA ELEVVVDATD LETYFEDVDA NEEDIMERPP VVTIMGHVDH
     GKTTLLDSIR NTRVTAGEAG GITQHIGAYQ IEYNDKPITF LDTPGHAAFT TMRARGAQVT
     DITILVVAAD DGVMPQTVEA INHAKAAEVP IIVAVNKIDK PTANPDRVMQ ELGEHGLYPE
     DWGGDTIFVQ LSAIKGDGID DLLEMIQLVT EVEELKANPK RTAIGTVIEA ELDKSRGPAA
     SLLVQDGTLE IGDSIVVGNT FGRVRAMVND LGKRIKTAGP SLPVEITGLQ DVPLAGDRFV
     VFKDEKKARR IGEARQQQNI LAQRQESQKV SLDNLFEQMK QGEMKDLNVI IKGDVQGSVE
     ALAASLMKID VEGVNVRIIH TAVGAINESD VTLASASNGI IIGFNVRPDV NAKRAAEAEG
     VDMRLHRIIY KVIEEIESAM KGMLDPEFEE KVIGQAEVRQ TINISKVGTV AGSYVTDGKI
     TRDSQVRIIR DGIVVYEGQV DALKRFKDDV REVAQGYECG ITIENFNDIK EGDIFEAFVM
     EEIKRA