IF2_CAMJR
ID IF2_CAMJR Reviewed; 871 AA.
AC Q5HX30;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CJE0131;
OS Campylobacter jejuni (strain RM1221).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=195099;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM1221;
RX PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
RA Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
RA Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
RA Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
RA Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
RA Nelson K.E.;
RT "Major structural differences and novel potential virulence mechanisms from
RT the genomes of multiple Campylobacter species.";
RL PLoS Biol. 3:72-85(2005).
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; CP000025; AAW34726.1; -; Genomic_DNA.
DR RefSeq; WP_002868393.1; NC_003912.7.
DR AlphaFoldDB; Q5HX30; -.
DR SMR; Q5HX30; -.
DR PRIDE; Q5HX30; -.
DR KEGG; cjr:CJE0131; -.
DR HOGENOM; CLU_006301_4_1_7; -.
DR OMA; NRDNRTG; -.
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..871
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137184"
FT DOMAIN 370..537
FT /note="tr-type G"
FT REGION 60..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..386
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 404..408
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 425..428
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 479..482
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 515..517
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 379..386
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 425..429
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 479..482
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 871 AA; 96120 MW; 3C8A31FA6306D76D CRC64;
MAKIRIHEIA KELGYDSKEI IEKANELGLG IKTASNAVEP EIAAAIYEYI QTREIPEAFK
KNIKTPTAKK PKKENIKEQE KLNESEKKEP KKEEKLKQEV KKEELKIEKE NAKEEEKQEI
IDAHKPQSLA SATLAKRRGL VIVKKKKDEE EIQVKKEEVK NSNDISINNE ERLSLKTMFS
NADESLKKKK KEKKSFVASK KESTEKMNFL DEHDFGDISL DDEDEVVLPD FSVKEQEKPQ
NINKKQPNFI RQAVGNSAGF GLEGGIQRRS RKKPSKKIEK KEVEEVGSVA ISKEIRVYEF
ADKIGKSTSE VISKLFMLGM MTTKNDFLDE DAIEILAAEF GIEINIINEA DEFDYVKDYE
EETDEKDLVT RAPVITIMGH VDHGKTSLLD YIRKSRVASG EAGGITQHVG AYMVEKNGRK
ITFIDTPGHE AFTAMRARGA SITDIVIIVV AADDGVKPQT KEAINHAKAA GVPIIIAINK
MDKEAANPDM VKTQLAEMEI MPVEWGGSYE FVGVSAKTGM GIEDLLEIVL LQADILELKA
NPKSFAKASI IESSVQKGRG AVATIIVQNG TLTIGSTVVA GEAYGKVRAM SDDQGKALKE
IKPGECGVIV GLSEVADAGE ILIAVKTDKE AREYANKRHE YNRQKELSKS TKVSIDELGA
KIKEGNLKAL PVILKADVQG SLEALKASLE KLRNDEIKVN IIHSGVGGIT QSDIELASAS
ENSIVLGFNI RPTGEVKERA KDKGVEIKTY NVIYNLLDDV KALLGGMMSP IISEEQLGQA
EIRQVINVPK IGQIAGCMVT EGVINRGAKI RLIRDGVVVY EGNVSSLKRF KDDAKEVAKG
YECGVGIEGC DDMRVGDYIE SYKEVEEQAS L
