IF2_CAMHC
ID IF2_CAMHC Reviewed; 914 AA.
AC A7I3V0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=CHAB381_1679;
OS Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 /
OS CH001A).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360107;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Nelson K.E.;
RT "Complete genome sequence of Campylobacter hominis ATCC BAA-381, a
RT commensal isolated from the human gastrointestinal tract.";
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; CP000776; ABS50985.1; -; Genomic_DNA.
DR RefSeq; WP_012109497.1; NC_009714.1.
DR AlphaFoldDB; A7I3V0; -.
DR SMR; A7I3V0; -.
DR STRING; 360107.CHAB381_1679; -.
DR EnsemblBacteria; ABS50985; ABS50985; CHAB381_1679.
DR KEGG; cha:CHAB381_1679; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_4_1_7; -.
DR OMA; VIFAMNK; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002407; 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; Reference proteome.
FT CHAIN 1..914
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335462"
FT DOMAIN 413..582
FT /note="tr-type G"
FT REGION 58..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..429
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 447..451
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 468..471
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 522..525
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 558..560
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 59..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 422..429
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 468..472
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 522..525
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 914 AA; 100601 MW; FC255421D4C94F90 CRC64;
MGVRISQIAD ELGYTSQEVV AKAQEMGYKR IKTGSNSVSD EEASAIYDYI QTGVLPKKTE
KKQTAKKSVK KDTVKKDTVK KTAVKKDDSK AAKKTKPIAK KSAPKTEKKV EKKVESKISK
PDNEILEAKP EISKPEIKAE PKKEEIEQKQ EAEPKIEVMP EKKSKIKSAF ARGETLASES
LKKRRGLVIV KKKKDLQTTE TQKIEAPKTQ KINLGLDAIF SNADANLKKK EKKKEKKQVQ
SKKVDTTKID LTSDRELADI RIDDDEDMVV LPDLTLKPIQ VEQKTKTKDQ PNIYKVSQNK
VYGNDGSIAR GARKKHKKAV KNSDNEIIKS IEIPKEIRLY EFAEKIKKQP SEIISKLFAL
GLMTTKNDFL DEDAIEILGA EFDIDIKIVD ENAKLNYVKV YDEQNLDDKN AVERVPVITI
MGHVDHGKTS LLDYIRNSRI ARGEAGGITQ HVGAYMVEKN GRKITFIDTP GHEAFTSMRA
RGAEVTDIVI IVVAADDGVK PQTKEAINHA KAAKVPIIIA INKMDKPTAN PDMVKSGLAE
LDIIPVEWGG KYEFVEISAK TGKGIEDLLE IVLLQADLLE LKASLNVPAK ATIIESSLQK
GRGPVATIIV QNGTLRVGDT VVAGVAYGKV RVINDDKGKK LKDIKPGECG VIVGLSEVPE
AGETLISVTS DKEAREYAKK IYEHNRQKEL SKSTKVTIDE LSAKIAEGEI KSLPVIVKAD
VVGSLEAVKS SLEKLRNDEV RVDIIHSGVG GITQNDVGLA SASENCIILG FNIRPTGEVK
ELAKERGVNI KTYNVIYNLI DDVKAVLGGL MSPIISEIEI GQAEIRQVIN VPKIGQIAGC
MVTDGSIQRG AKIRVIREGV IKFEGNVSSL KRFKDDVKEV AKGFECGVGI EGYNDMQVGD
FIESFKEKEE IASL
