ID IF2_CAMC5 Reviewed; 903 AA.
AC A7GZZ3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
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=Ccur92_14810; ORFNames=CCV52592_0355;
OS Campylobacter curvus (strain 525.92).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360105;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=525.92;
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 "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT feces.";
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; CP000767; EAT99580.2; -; Genomic_DNA.
DR RefSeq; WP_011992627.1; NC_009715.2.
DR AlphaFoldDB; A7GZZ3; -.
DR SMR; A7GZZ3; -.
DR STRING; 360105.CCV52592_0355; -.
DR KEGG; ccv:CCV52592_0355; -.
DR HOGENOM; CLU_006301_4_1_7; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000006380; 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; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 1.10.10.2480; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
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..903
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008220"
FT DOMAIN 402..569
FT /note="tr-type G"
FT REGION 57..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..418
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 436..440
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 457..460
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 511..514
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 547..549
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 57..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 411..418
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 457..461
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 511..514
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 903 AA; 99189 MW; B2F2F1F275E57608 CRC64;
MSNVRISEIA NELGYPSKEI VEKAQELGLK VKTHSNAVSL EEAEAIYEYV QSGVIPEKFK
KEKPKAKPKK EAKEPSEKEV GKKQTKAKEE KPAKASTTQK KDTKSHKIGE TKAKKDQESV
KKQKVEVQPK QEQTKQELQP KEAEFKSEVK DEISEPQKPK ESLADVSQRR RGLMIVKKKK
EFESAPVRRD ENRVKSTDAV EINSLKNMFA SSDENLARKK KKDKKPVVAT KKDSAQKMDL
LGSSDFGDIV IEDEDVVVLP DFSFKTPTPQ PMQKTKQPNV LKPTINNTIN PFGEGGIQRR
ARKKHKKPEN KQNSEAVTSI NIPKEIRVYE FAEKLNKQPS EIIGKLFMLG MMTTKNDFLD
EDAIEILADE FNVEVNIIDD QKEFDYVAAY EEEVRDDENL LPRAPVITIM GHVDHGKTSL
LDYIRKSRVA AGEAGGITQH VGAYMVNKNG KNITFIDTPG HEAFTAMRAR GAGVTDIVII
VVAADDGVKP QTKEAVNHAK AAGVPIIIAI NKMDKEAANP DLVKTGLAEL DIMPTEWGGK
YEFVPISAKT GMGIDDLLEI VLLQAEILEL KANPKASAKA SVIESSLQKG RGPVATIIVE
NGTLRVGDTV VAGVAYGKIR SLLDDQGRPL QEIKPGECGV IVGLSEIAEA GETLIGVKTD
KEAREYAQKK AEYLRQKELS KSTKVSLDEL SAKIAEGELK TLPVIVKADV GGSLEALKAS
LEKLANNEIK VDIIHSGVGG ITQSDVALAS ASKDCVILGF NIRPTGEIKE KAKESGVEIK
TYNVIYNLID DVKALLGGLM SPIIREEQLG QAQVRQVINV PKIGAIAGCL VTEGTINRGA
KIRLIRDGVV VYEGMVSSLK RFKDDVKEVA KGYECGVGIE GCNDIRENDY IESFKEIEEQ
AKL
//
