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IF2_SYNWW
ID   IF2_SYNWW               Reviewed;         882 AA.
AC   Q0AYI8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Swol_0900;
OS   Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=335541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2245B / Goettingen;
RX   PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA   Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA   McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT   "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT   metabolism and biohydrogen production.";
RL   Environ. Microbiol. 12:2289-2301(2010).
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; CP000448; ABI68216.1; -; Genomic_DNA.
DR   RefSeq; WP_011640321.1; NC_008346.1.
DR   AlphaFoldDB; Q0AYI8; -.
DR   SMR; Q0AYI8; -.
DR   STRING; 335541.Swol_0900; -.
DR   PRIDE; Q0AYI8; -.
DR   EnsemblBacteria; ABI68216; ABI68216; Swol_0900.
DR   KEGG; swo:Swol_0900; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_9_2_9; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000001968; 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; 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; Reference proteome.
FT   CHAIN           1..882
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008366"
FT   DOMAIN          383..556
FT                   /note="tr-type G"
FT   REGION          38..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          392..399
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          417..421
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          438..441
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          492..495
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          528..530
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        45..75
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         392..399
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         438..442
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         492..495
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   882 AA;  97143 MW;  1C6F1C469A0FA607 CRC64;
     MAKIRVHELA KELGIASKEM VEVLVELGLD VKNHMSTIED SQASWVKKRL SKSDEDSKKQ
     PAQPVTRDEA VKKHSGEPAT QTTQKKPDNP RHVSGPRPQE GSKPSGSTGR REFSENREQS
     RKGEERHSAN PRPGTQMKSP RNNAPRPTTR PENRSAGATG RTDNRAPGAA GRTDNRAPGA
     VGRTDNRGAG SASRPDNRVT RPAAGRPDNK GSRPSDAKRP PQRTVPGNTP RPVSSPERTT
     EKKPGEASRT LPGGAKTAGD KKAFRKNTPA FGQYQSKDYS RPGRKSKHKR KKENIEFQTP
     ENIKIEGSIM VRDLAEKLNK NPAEIMKKLM ELGIMATINQ NIDFETAEIV SSLYDVKVER
     ELSEEEKILE ELVDIDDDAE LIARPPVVTI MGHVDHGKTS LLDRIRQANV VSGEAGGITQ
     HIGAYQVTIK NNKITFIDTP GHEAFTAMRA RGANLTDIVI LVVAADDGVM PQTVEAINHI
     RAAKVPFLVA INKIDKPQAD PERIKQQLTE YNIVPEEWGG DTIFVPVSAK SGEGIENLLE
     MILLVAEMNE IRANPDRAAY GLVVEGELDK GRGAVATVLV LNGTLNIGDY IICGTNWCRV
     RAMIDDRGKR VDKALPSMPV EIMGWSGVPE AGGKVQVCDE KVAKEIIGLR LSEKKIEEQK
     QSSRVSLDEF FQQMKDAEVK ELTLIIKGDV QGSVEALRQS LLRLATNEVK VNVIHSAVGA
     ITETDVMLAS ASNAIIIGFN VRPDSKARKY AEDEKIDVRM YRVIYEAIDD VKKAMSGLLD
     PEYKEKFLGR AEVRALFKVP HVGVIAGSYV IDGKIQRNAS VRVLRDGVIV YEGQLSSLKR
     FKDDAKEVVE NYECGIGIKD FNDVKEGDII EAYTLEEIPR EL
 
 
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