IF2_CAMLR
ID IF2_CAMLR Reviewed; 877 AA.
AC B9KEV0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, 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}; OrderedLocusNames=Cla_0222;
OS Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=306263;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM2100 / D67 / ATCC BAA-1060;
RX PubMed=18713059; DOI=10.1089/fpd.2008.0101;
RA Miller W.G., Wang G., Binnewies T.T., Parker C.T.;
RT "The complete genome sequence and analysis of the human pathogen
RT Campylobacter lari.";
RL Foodborne Pathog. Dis. 5:371-386(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; CP000932; ACM63585.1; -; Genomic_DNA.
DR RefSeq; WP_012660969.1; NC_012039.1.
DR AlphaFoldDB; B9KEV0; -.
DR SMR; B9KEV0; -.
DR STRING; 306263.Cla_0222; -.
DR PRIDE; B9KEV0; -.
DR EnsemblBacteria; ACM63585; ACM63585; CLA_0222.
DR GeneID; 7410945; -.
DR KEGG; cla:CLA_0222; -.
DR PATRIC; fig|306263.5.peg.221; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_4_1_7; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000007727; 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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 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..877
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000118754"
FT DOMAIN 376..543
FT /note="tr-type G"
FT REGION 66..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..392
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 410..414
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 431..434
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 485..488
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 521..523
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 242..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 385..392
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 431..435
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 485..488
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 877 AA; 96556 MW; 0DF9BB4FDF41CA67 CRC64;
MADVKISEIA QELGYTSKEI IEKANEMGLE DIKSPNKKVS SEIAEAIYQY VQSGEILDVV
KKIAKPKKES TAKKTTKKDE VKKEEKKTTT KKESKNPAKA VSEKKDEVKK EEKQPENPIK
NEILEEKKEE IKLDEKLGSN LNLAKRRGLV IVKKKKEESN ETQINNEEKI STQATQGLSL
SMIFSNSDES LKRKKKEKKN HPVASKKENT TKMDLLGDKD FADISLEDDD MVVLPDFSIK
ENKPAQPTNK KQPNILKQSL NNSINPFGEG GIQRRSRKKP PKKVEKKESE AITSVSIPKE
IRVYEFAEKL GKNTGEIISK LFMLGMMTTK NDFLDEDAIE ILAAEFGVEI NIIDEADEFD
YVKDYDENQT EENLSQRAPV ITIMGHVDHG KTSLLDYIRK SRIASGEAGG ITQHVGAYMV
EKNGRKITFI DTPGHEAFTA MRARGASITD IVIIVVAADD GVKPQTKEAI NHAKAANVPI
IIAINKMDKE NANPDMVKTQ LAEMEIMPVE WGGSHEFVPV SAKKGDGVED LLEIVLLQAD
ILELKANPKA HAKASIIESS VQKGRGPVAT IIVQNGTLRV GNTVVAGEAY GKVRAMSDDQ
GKALKEIGPG ECGVIIGLSE VADAGETLIA VDSDKQAREY ANKRHEYNRQ KELSKSTKVS
IDELGAKIKE GNLKALPVIL KADVQGSLEA IKASLEKLKN DEIKVNIIHS GVGGITQSDI
ELASASENSI VLGFNIRPTG EIKERAKDKG VEIKTYNVIY NLLDDVKALL GGMMSPIISE
EQLGQAEIRQ VINVPKLGQI AGCMVTEGTI NRGAKIRLIR DGVVVFEGNV SSLKRFKDDV
REVAKGYECG VGIEGCNDMR VGDYIESYKE VEEQVSL
