IF2_CAMJD
ID IF2_CAMJD Reviewed; 854 AA.
AC A7H1L5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=JJD26997_0149;
OS Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 /
OS 269.97).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1458 / RM4099 / 269.97;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97
RT isolated from human blood.";
RL Submitted (JUL-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; CP000768; ABS43395.1; -; Genomic_DNA.
DR AlphaFoldDB; A7H1L5; -.
DR SMR; A7H1L5; -.
DR EnsemblBacteria; ABS43395; ABS43395; JJD26997_0149.
DR KEGG; cjd:JJD26997_0149; -.
DR HOGENOM; CLU_006301_4_1_7; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000002302; 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..854
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008222"
FT DOMAIN 353..520
FT /note="tr-type G"
FT REGION 61..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..369
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 387..391
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 408..411
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 462..465
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 498..500
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 61..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 362..369
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 408..412
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 462..465
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 854 AA; 94080 MW; F7BB8282047D1653 CRC64;
MAKIRIHEIA KELGYDSKEI IEKANELGLG IKTASNAVEP DIAVAIYEYI QTREIPEAFK
KNIKTPTAKK PKKENAKDQE KLNESEKKEP KKEESKEQEK QEIIDTHKPQ SLASATLAKR
RGLVIVKKKK DEEEIQVKKE EIKNSNDISI NNEERLSLKT MFSNADESLK KKKKEKKSFV
ASKKESTEKM NFLDEHDFGD ISLDDEDEVV LPDFSVKEQE KPQNINKKQP NFIRQAVGNS
AGFGLEGGIQ RRSRKKPPKK IEKKEVEEVS SVSISKEIRV YEFADKIGKS TSEVISKLFM
LGMMTTKNDF LDEDAIEILA AEFGIEINII NEADEFDYVK DYEEETDEKD LVTRAPVITI
MGHVDHGKTS LLDYIRKSRV ASGEAGGITQ HVGAYMVEKN GRKITFIDTP GHEAFTAMRA
RGASITDIVI IVVAADDGVK PQTKEAINHA KAAGVPIIIA INKMDKEAAN PDMVKTQLAE
MEIMPVEWGG SYEFVGVSAK TGMGIEDLLE IVLLQADILE LKANPKSFAK ASIIESSVQK
GRGAVATIIV QNGTLAVGST VVAGEAYGKV RAMSDDQGKA LKEIKPGECG VIVGLSEVAD
AGEILIAVKT DKEAREYANK RHEYNRQKEL SKSTKVSIDE LGAKIKEGNL KALPVILKAD
VQGSLEALKA SLEKLRNDEI KVNIIYSGVG GITQSDIELA SASENSIVLG FNIRPTGEVK
ERAKDKGVEI KTYNVIYNLL DDVKALLGGM MSPIISEEQL GQAEIRQVIN VPKIGQIAGC
MVTEGVINRG AKIRLIRDGV VVYEGNVSSL KRFKDDAKEV AKGYECGVGI EGCDDMRVGD
YIESYKEVEE QASL
