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IF2_CAMC1
ID   IF2_CAMC1               Reviewed;         885 AA.
AC   A7ZC69;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN   OrderedLocusNames=Ccon26_04760; ORFNames=CCC13826_1495;
OS   Campylobacter concisus (strain 13826).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13826;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., On S., Nelson K.E.;
RT   "Genome sequence of Campylobacter concisus 13826 isolated from human
RT   feces.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000792; EAT99040.1; -; Genomic_DNA.
DR   RefSeq; WP_012001357.1; NC_009802.2.
DR   AlphaFoldDB; A7ZC69; -.
DR   SMR; A7ZC69; -.
DR   STRING; 360104.CCC13826_1495; -.
DR   EnsemblBacteria; EAT99040; EAT99040; CCC13826_1495.
DR   KEGG; cco:CCC13826_1495; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_4_1_7; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000001121; 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.
FT   CHAIN           1..885
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008219"
FT   DOMAIN          384..553
FT                   /note="tr-type G"
FT   REGION          55..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          393..400
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          418..422
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          439..442
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          493..496
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          529..531
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         393..400
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         439..443
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         493..496
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   885 AA;  96941 MW;  8A1AADE7F6978261 CRC64;
     MSNVRISEIA NELGYPSKEI VEKAQELGLK VKTHSNAVSL EEAEAIYEYV QTGVIPDKFK
     KKKSEPKAKK EPKKETEKEP AKKEEKPKTE PKKAATKAEP KPEKAKAEPK KEAQISEEKP
     KTEPKKEEPV KVEQKPAEAP KPKESLADVT QKRRGLVIVK KKKDYEAPAP IKEEKKAEAA
     VTNISDFKSM FSASDENLAR KKKKEKKVTV VSKKDSAEKM DLLGGSDFGD IVLEDEDVVV
     LPDFSFKTPA PTPMQRTKQP NAMKTTVNNT INSFGEGGIQ RRARKKHKKP ENKQNSEAVT
     SINIPKEIRV YEFAEKLNKQ PSEVIGKLFM LGMMTTKNDF LDEDAIEILA DEFNVEVNII
     DDQKEFDYVA AYEEEIKDDE NLQPRAPVIT IMGHVDHGKT SLLDYIRKSR VAAGEAGGIT
     QHVGAYMVNK NGRNITFIDT PGHEAFTAMR ARGAGVTDIV IIVVAADDGV KPQTKEAVSH
     AKAAGVPIII AINKMDKESA NPDLVKTGLA ELDIMPTEWG GKYEFVPISA KTGMGIDDLL
     EIVLLQADLL ELKANPKANA KATVIESSLQ KGRGPVATII VENGTLHVGD TVVAGVAYGK
     IRSLLDDQGR SLREIKPGEC GVIVGLSEIA EAGETLIGVK TDKEAREYAQ KKAEYIRQKE
     LSKSTKVSID ELSAKIAEGE LKTLPVIIKA DVGGSLEALK ASLEKLANDE IRVNVIHSGV
     GGITQSDVAL ASASNDCIIL GFNIRPTGEI KEKAKESGVE IKTYNVIYNL IDDVKAILGG
     LMSPIIREEQ LGQAQVRQVI HVPKVGTIAG CIVTEGTINR GAKIRLIREG VVVYEGLVSS
     LKRFKDDVKE VAKGYECGVG IENFNDIREN DYIESFKEVK EKATL
 
 
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