ID   IF2_CAMJ8               Reviewed;         871 AA.
AC   A8FJU1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=C8J_0129;
OS   Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC
OS   11828).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=407148;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81116 / NCTC 11828;
RX   PubMed=17873037; DOI=10.1128/jb.01404-07;
RA   Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M.,
RA   van Vliet A.H.M.;
RT   "The complete genome sequence of Campylobacter jejuni strain 81116
RT   (NCTC11828).";
RL   J. Bacteriol. 189:8402-8403(2007).
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; CP000814; ABV51728.1; -; Genomic_DNA.
DR   RefSeq; WP_002893398.1; NC_009839.1.
DR   AlphaFoldDB; A8FJU1; -.
DR   SMR; A8FJU1; -.
DR   KEGG; cju:C8J_0129; -.
DR   HOGENOM; CLU_006301_4_1_7; -.
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..871
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000071287"
FT   DOMAIN          370..537
FT                   /note="tr-type G"
FT   REGION          60..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          184..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          379..386
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          404..408
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          425..428
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          479..482
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          515..517
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         379..386
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         425..429
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         479..482
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   871 AA;  96160 MW;  9FD730BBB088F6EE CRC64;
     MAKIRIHEIA KELGYDSKEI IEKANELGLG IKTASNAVEP EIAAAIYEYI QTREIPEAFK
     KNIKTPTAKK PKKENIKEQE KLNESEKKEP KKEEKLKQEV KKEELKVEKE NVKEEEKQEI
     IDAHKPQSLA SATLAKRRGL VIVKKKKDEE EIQVKKEEVK NSNDISINNE ERLSLKTMFS
     NADESLKKKK KEKKSFVASK KESTEKMNFL DEHDFGDISL DDEDEVVLPD FSVKEQEKPQ
     NINKKQPNFI RQAVGNSAGF GLEGGIQRRS RKKPPKKIEK KEVEEVSSVA ISKEIRVYEF
     ADKIGKSTSE VISKLFMLGM MTTKNDFLDE DAIEILAAEF GIEINIINEA DEFDYVKDYE
     EETDEKDLVT RAPVITIMGH VDHGKTSLLD YIRKSRVASG EAGGITQHVG AYMVEKNGRK
     ITFIDTPGHE AFTAMRARGA SITDIVIIVV AADDGVKPQT KEAINHAKAA GVPIIIAINK
     MDKEAANPDM VKTQLAEMEI MPVEWGGSYE FVGVSAKTGM GIEDLLEIVL LQADILELKA
     NPKSFAKASI IESSVQKGRG AVATIIVQNG TLTVGSTVVA GEAYGKVRAM SDDQGKALKE
     IKPGECGVIV GLSEVADAGE ILIAVKTDKE AREYANKRHE YNRQKELSKS TKVSIDELGA
     KIKEGNLKAL PVILKADVQG SLEALKASLE KLRNDEIKVN IIHSGVGGIT QSDIELASAS
     ENSIVLGFNI RPTGEVKERA KDKGVEIKTY NVIYNLLDDV KALLGGMMSP IISEEQLGQA
     EIRQVINVPK IGQIAGCMVT EGVINRGAKI RLIRDGVVVY EGNVSSLKRF KDDAKEVAKG
     YECGVGIEGC DDMRVGDYIE SYKEVEEQAS L