ID IF2_MYCPN Reviewed; 617 AA.
AC P75590;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 27-MAR-2024, entry version 139.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB; OrderedLocusNames=MPN_155; ORFNames=MP676;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1)
OS (Mycoplasmoides pneumoniae).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC Mycoplasmoides.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129 / Subtype 1;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
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DR EMBL; U00089; AAB96324.1; -; Genomic_DNA.
DR PIR; S74002; S74002.
DR RefSeq; NP_109843.1; NC_000912.1.
DR RefSeq; WP_010874512.1; NZ_OU342337.1.
DR AlphaFoldDB; P75590; -.
DR SMR; P75590; -.
DR IntAct; P75590; 8.
DR STRING; 272634.MPN_155; -.
DR EnsemblBacteria; AAB96324; AAB96324; MPN_155.
DR KEGG; mpn:MPN_155; -.
DR PATRIC; fig|272634.6.peg.173; -.
DR HOGENOM; CLU_006301_5_1_14; -.
DR OrthoDB; 9811804at2; -.
DR BioCyc; MPNE272634:G1GJ3-262-MONOMER; -.
DR Proteomes; UP000000808; 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; IPR004161; EFTu-like_2.
DR InterPro; IPR044145; IF2_II.
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; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
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..617
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137222"
FT DOMAIN 119..288
FT /note="tr-type G"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..135
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 153..157
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 175..178
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 229..232
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 265..267
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 128..135
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 175..179
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 229..232
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 617 AA; 67897 MW; B658142123D70133 CRC64;
MSKHKPRHFQ KNKFDNRAKT SAKQQFRQVK TGVKDGVFVY KGPLTVSEFC LKTNIPTANI
IKHFFLNGVP LTLNSVLSTE QLADACVNFG FDFKVETEIT HDNIISNIKF DDDPTQLSPR
PPIVTIMGHV DHGKTSLLDA IRQTNTAAKE FGGITQKIGA YQVKNQEGKT ITFIDTPGHE
AFTGMRARGA QVTDIVVLVV AGDDGLKQQT EEAISHAKSA KTPIIVFINK MDKPTANPDM
VIQQLNKFDL VPEEWGGDTI FVKGSALTKE GIQELLDSIL LVAEVEDYKA NFNAHSSGYA
IEVQTTKGLG PTATIIVKRG TLKIGDIVVL GPAWGKVRTM QDENGVHLQE AMPSKPVQIS
GFDIVPVAGE KFIVFDDEKD AKLIANKFRE QQKQKLNTTQ INEELKQKIK SKEIKVLNLI
FKVDSDGSLA AIKQAMQSID VPGMSVNIIH SGVGLISEND IMLAKASGAL LFSLNLGLSQ
VVKNIASLQG VKVDVHYHIP KLAEEIENIL KGQLEPVYED VELGRAEVLQ LWYHSKVGHI
AGTLVKTGKV KRGALCKLLR RNETIYEGRV DSLKSEKNPV NQMEAGKNCG IVINGCEDIQ
VCDIILVYEK QEVKSKS
//
