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IF2_MYCS5
ID   IF2_MYCS5               Reviewed;         602 AA.
AC   Q4A578;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=MS53_0686;
OS   Mycoplasmopsis synoviae (strain 53) (Mycoplasma synoviae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=262723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=53;
RX   PubMed=16077101; DOI=10.1128/jb.187.16.5568-5577.2005;
RA   Vasconcelos A.T.R., Ferreira H.B., Bizarro C.V., Bonatto S.L.,
RA   Carvalho M.O., Pinto P.M., Almeida D.F., Almeida L.G.P., Almeida R.,
RA   Alves-Junior L., Assuncao E.N., Azevedo V.A.C., Bogo M.R., Brigido M.M.,
RA   Brocchi M., Burity H.A., Camargo A.A., Camargo S.S., Carepo M.S.,
RA   Carraro D.M., de Mattos Cascardo J.C., Castro L.A., Cavalcanti G.,
RA   Chemale G., Collevatti R.G., Cunha C.W., Dallagiovanna B., Dambros B.P.,
RA   Dellagostin O.A., Falcao C., Fantinatti-Garboggini F., Felipe M.S.S.,
RA   Fiorentin L., Franco G.R., Freitas N.S.A., Frias D., Grangeiro T.B.,
RA   Grisard E.C., Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A.,
RA   Laurino J.P., Lima L.F.A., Lopes M.I., Loreto E.L.S., Madeira H.M.F.,
RA   Manfio G.P., Maranhao A.Q., Martinkovics C.T., Medeiros S.R.B.,
RA   Moreira M.A.M., Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C.,
RA   Paixao R.F.C., Pedrosa F.O., Pena S.D.J., Pereira M., Pereira-Ferrari L.,
RA   Piffer I., Pinto L.S., Potrich D.P., Salim A.C.M., Santos F.R., Schmitt R.,
RA   Schneider M.P.C., Schrank A., Schrank I.S., Schuck A.F., Seuanez H.N.,
RA   Silva D.W., Silva R., Silva S.C., Soares C.M.A., Souza K.R.L., Souza R.C.,
RA   Staats C.C., Steffens M.B.R., Teixeira S.M.R., Urmenyi T.P.,
RA   Vainstein M.H., Zuccherato L.W., Simpson A.J.G., Zaha A.;
RT   "Swine and poultry pathogens: the complete genome sequences of two strains
RT   of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae.";
RL   J. Bacteriol. 187:5568-5577(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; AE017245; AAZ44093.1; -; Genomic_DNA.
DR   RefSeq; WP_011283822.1; NC_007294.1.
DR   AlphaFoldDB; Q4A578; -.
DR   SMR; Q4A578; -.
DR   STRING; 262723.MS53_0686; -.
DR   PRIDE; Q4A578; -.
DR   EnsemblBacteria; AAZ44093; AAZ44093; MS53_0686.
DR   GeneID; 61970933; -.
DR   KEGG; msy:MS53_0686; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_14; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000000549; 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; 1.
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.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..602
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000232591"
FT   DOMAIN          112..281
FT                   /note="tr-type G"
FT   REGION          121..128
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          146..150
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          167..170
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          221..224
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          257..259
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         121..128
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         167..171
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         221..224
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   602 AA;  67225 MW;  C88A02DE20EEB7F2 CRC64;
     MSKKKTNRKN NIDDIKNQLQ NAKTELKNGT FFFTGKMSIF EFANKTNLNA NEIVKNFFLA
     GKLYNINHIL EEEEIAQLCI ENNFEFSKET KIDGTNFLDE ISFEDKPEDL IKRAPIITIM
     GHVDHGKTSL IDKIRNSNIT KSESSGITQH TGAYQIVHKN QKITFIDTPG HEAFSAMRAR
     GANVTDIVVL VVAADDGVMP QTVEAIKHCK NANVPIIVFV NKMDKPNKDL DKLKGQLAEN
     GVVIEEYGGS VQTAYGSALK NEGIKELFDE ILLLCEVLDL KANPKRFPIG TVIESRVDKR
     IGALTTIIVQ NGTLYKGDFL LVGSQYSKIR TLSDENGNAM DSIEPGCPAV VTGFKIPPTA
     GSKFVGINDE KFAKRLASEK NYQEKINNLY SLSNSNNNSG GKKVINVIIK SDTNGTAEAI
     KNQLEYLEND EAKIKVISSN VGDITENDLM LAKASDSIIF TFNLKVLPTI RENLKVKKIT
     LISHNVIYKI IEDCKLILDE HVTPIYEEKK IGQAHVIKIF TYSKLGTIAG SMQDTGVVRL
     GAKVKVYRKN KLIHEGFVQT LKRNLNEVKE VEKGKDFGTH LKDFNNIEVD DVLEFYEDVR
     VN
 
 
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