IF2_CAMFF
ID IF2_CAMFF Reviewed; 838 AA.
AC A0RQZ4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=CFF8240_1493;
OS Campylobacter fetus subsp. fetus (strain 82-40).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=82-40;
RA Fouts D.E., Nelson K.E.;
RT "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL Submitted (NOV-2006) 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; CP000487; ABK82048.1; -; Genomic_DNA.
DR RefSeq; WP_002850489.1; NC_008599.1.
DR AlphaFoldDB; A0RQZ4; -.
DR SMR; A0RQZ4; -.
DR STRING; 360106.CFF8240_1493; -.
DR PRIDE; A0RQZ4; -.
DR EnsemblBacteria; ABK82048; ABK82048; CFF8240_1493.
DR GeneID; 61065310; -.
DR KEGG; cff:CFF8240_1493; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_4_1_7; -.
DR OMA; DHPLREY; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000760; 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..838
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008221"
FT DOMAIN 337..506
FT /note="tr-type G"
FT REGION 50..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..353
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 371..375
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 392..395
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 446..449
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 482..484
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 54..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 346..353
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 392..396
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 446..449
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 838 AA; 91824 MW; 037150BB5C34B025 CRC64;
MANIRIHEIA KELGYSNKEI LEKAKELGFK VTTSSSAVTP EDAAQLYDYV QSGKKPESPE
KKDIKQNTQK EAPETQTQQK PIEQEVETKQ NIDSTPIKVE PKQESLASST LSKRRGLVIV
KKKKVEVQPI QKQQSEPINK GLEAIFGSSD ENLKKKKKEK KPIIATKKEN SAKIDLLSAI
SFSDDISIDD EDVVVLPDLT VKPIEIERQN TVKKQINVYK TSQNNSFSFE GGIQRNSRKK
HKKVVKDKDN EDISSVDIPK EIRLYEFADK IKKSSSEVIA KLFILGKMTT KNDFLEEDEI
EILGAEFGIE VNIVDTKEDF DYVKAYEDEI LEDNSVSRAP VVTIMGHVDH GKTSLLDYIR
NSRVASGEAG GITQHVGAYM VEKSGKNITF IDTPGHEAFT AMRARGASVT DIVIIVVAAD
DGVKPQTKEA INHAKAAGVP IIIAINKMDK ESANPDLVKT GLAELDILPT EWGGGYEFVP
ISAKTGIGIE DLLEIVLLQA ELLELKANPD REAKATIIES SLQKGRGPVA TAIVENGTLR
VGDTIVAGVA YGKVRALQDD KGNSLKSIKP GECGVIIGLS EVPDAGETLI SVKTDKEARE
YAQKKYDYLR QKELSKSTKV TIDELSAKIA EGELKSLPVI IKADVQGSLE AIKASLEKLK
NDEIKVDIIH SGVGGISQSD ITLASASSNC VILGFNIRPT GDVKEKAKER SVEIKTYNVI
YNLIDDVKAL LSGLMSPIIS EEELGQAVIR QVINVPKIGQ IAGCMVTDGS INRGAKIRVI
RDGVVVFEGN VSSLKRFKDD VKEVAKGYEC GVGIEGYNDM REGDYIESYK EVESKVEL
