ID   IF2_STAA1               Reviewed;         705 AA.
AC   A7X1Q1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SAHV_1259;
OS   Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=418127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu3 / ATCC 700698;
RX   PubMed=17954695; DOI=10.1128/aac.00534-07;
RA   Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT   "Mutated response regulator graR is responsible for phenotypic conversion
RT   of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT   resistance to vancomycin-intermediate resistance.";
RL   Antimicrob. Agents Chemother. 52:45-53(2008).
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; AP009324; BAF78142.1; -; Genomic_DNA.
DR   RefSeq; WP_000043635.1; NC_009782.1.
DR   AlphaFoldDB; A7X1Q1; -.
DR   SMR; A7X1Q1; -.
DR   KEGG; saw:SAHV_1259; -.
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..705
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008345"
FT   DOMAIN          207..376
FT                   /note="tr-type G"
FT   REGION          40..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          216..223
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          241..245
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          262..265
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          316..319
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          352..354
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        40..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         216..223
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         262..266
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         316..319
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   705 AA;  77857 MW;  0BA5ED8E97BC24FC CRC64;
     MSKQRIYEYA KELNLKSKEI IDELKSMNIE VSNHMQALED DQIKALDKKF KKEQKNDNKQ
     STQNNHQKSN NQNQNKGQQK DNKKNQQQNN KGNKGNKKNN RNNKKNNKNN KPQNQPAAPK
     EIPSKVTYQE GITVGEFADK LNVESSEIIK KLFLLGIVAN INQSLNQETI ELIADDYGVE
     VEEEVVINEE DLSIYFEDEK DDPEAIERPA VVTIMGHVDH GKTTLLDSIR HTKVTAGEAG
     GITQHIGAYQ IENDGKKITF LDTPGHAAFT TMRARGAQVT DITILVVAAD DGVMPQTIEA
     INHAKEAEVP IIVAVNKIDK PTSNPDRVMQ ELTEYGLIPE DWGGETIFVP LSALSGDGID
     DLLEMIGLVA EVQELKANPK NRAVGTVIEA ELDKSRGPSA SLLVQNGTLN VGDAIVVGNT
     YGRIRAMVND LGQRIKTAGP STPVEITGIN DVPQAGDRFV VFSDEKQARR IGESRHEASI
     VQQRQESKNV SLDNLFEQMK QGEMKDLNVI IKGDVQGSVE ALAASLMKID VEGVNVRIIH
     TAVGAINESD VTLANASNGI IIGFNVRPDS GAKRAAEAEN VDMRLHRVIY NVIEEIESAM
     KGLLDPEFEE QVIGQAEVRQ TFKVSKVGTI AGCYVTEGKI TRNAGVRIIR DGIVQYEGEL
     DTLKRFKDDA KEVAKGYECG ITIENYNDLK EGDVIEAFEM VEIKR