ID IF2_MESH2 Reviewed; 599 AA.
AC Q5ZZV6;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=mhp601;
OS Mesomycoplasma hyopneumoniae (strain 232) (Mycoplasma hyopneumoniae).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Metamycoplasmataceae;
OC Mesomycoplasma.
OX NCBI_TaxID=295358;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=232;
RX PubMed=15489423; DOI=10.1128/jb.186.21.7123-7133.2004;
RA Minion F.C., Lefkowitz E.J., Madsen M.L., Cleary B.J., Swartzell S.M.,
RA Mahairas G.G.;
RT "The genome sequence of Mycoplasma hyopneumoniae strain 232, the agent of
RT swine mycoplasmosis.";
RL J. Bacteriol. 186:7123-7133(2004).
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; AE017332; AAV27988.1; -; Genomic_DNA.
DR RefSeq; WP_011206432.1; NC_006360.1.
DR AlphaFoldDB; Q5ZZV6; -.
DR SMR; Q5ZZV6; -.
DR KEGG; mhy:mhp601; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_14; -.
DR PhylomeDB; Q5ZZV6; -.
DR Proteomes; UP000006822; 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; 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; 1.
DR PRINTS; PR00315; ELONGATNFCT.
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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..599
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000232585"
FT DOMAIN 111..278
FT /note="tr-type G"
FT REGION 120..127
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 145..149
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 166..169
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 220..223
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 256..258
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 120..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 166..170
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 220..223
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 599 AA; 66818 MW; B86A6B60BA0C9713 CRC64;
MKKSQKRISN VSEIKAQLKT VETKVHNGVF LFSGIMTIAE LAQKINVSVN QIITYFFHQA
KMYNLNHSLS EDEIAEICLE FGLDFKKEVQ IDASNFMEEV SILDQDKDLS PRPPIITVMG
HVDHGKTTLL DYIRKTNIAK NEKGGITQHT GAYQVVFQGH IINFIDTPGH EAFTQMRARG
AKVTDIIVLV VAADDGVMPQ TKEAINHAAA ANVPIIVFVN KMDKPNKDVD RIKNELSALN
IVTEEWGGSN IFVYGSALTG QGIDTLFSSI LLLAEILELK ANKNRYPIGT VIEAKLHHNK
GTIATLMVQN GTLMVRDFIV AGYQYGRIRS LENTNGQPIK FAPPGTPVIV TGLNYVPEAG
DKFFGFHEEK FAKQLALERK QSEKISKTKV QTKQQTKEKT LNIIIKADVA GIAQALHSTI
EKLASKQVHI HILHSGVGIV NKADILLAQT SNSIIYAFNL QIPAAIKAQA KQAQVEIREH
TIIYKIVDEI KKQVRGMREI RYELQQIGTA KIIAKFWFSK VGSIAGCSVL SGKFVENCKI
ELWRNSKLIH SGKIESLQRD KNPVKEVQVG NEFGTHIYKF NDIEIGDELK AFLDVEIEE
//
