IF2_GLUOX
ID IF2_GLUOX Reviewed; 917 AA.
AC Q5FQM3;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=GOX1582;
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H;
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(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; CP000009; AAW61323.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5FQM3; -.
DR SMR; Q5FQM3; -.
DR STRING; 290633.GOX1582; -.
DR PRIDE; Q5FQM3; -.
DR EnsemblBacteria; AAW61323; AAW61323; GOX1582.
DR KEGG; gox:GOX1582; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000006375; 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; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 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.
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..917
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228202"
FT DOMAIN 416..586
FT /note="tr-type G"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..432
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 450..454
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 472..475
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 526..529
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 562..564
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..275
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 425..432
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 472..476
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 526..529
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 917 AA; 98526 MW; 0E5D34A3AC1B4352 CRC64;
MSDGNERNQD GNNTPSQGGE QTRSSRLSLR PAGRQEVGRT VDAGSVRQSF SHGRSKVVQV
EVRKPKRNAA GPGAGAAARG GRAGGRALTA AELAARQRAL ELQRKAAAEE AARREEEKIQ
IMSAAEAARR AAEEERLISE QKAAEIAALK ESEQQAAREQ AAAEAAARAA EQAAAEAAAR
EAEEAARSAP LDPRSHSTGG VQLAAPVQRL RPLAERAIMP PRPVQPSRPA AAAPARNNET
LHLRSGAAAG GDDERRPAPR RSGPGAPPAP PRRPSAPSRK GGGSDRRSGR IDVRAAIEGD
DDKTRSLASV RRQRDRERRQ AELERLRSDQ VRVVRDVIVP ETITVAELAN RMAARQGEVI
KALMKMGVMA TAAQSIDGDT AELVVEEFGH RIKRVSESDV EIGIEGVEDN ADDLKPRAPV
VTVMGHVDHG KTSLLDALRT TDVAASEAGG ITQHIGAYQI TAPSGKKITF IDTPGHEAFT
SMRARGASVT DIVVLVVAAD DGVMPQTIEA IKHAKAANAP IIVAINKIDK PGANPNRVRQ
ELLNHEIVVE EMGGDTQDVE VSALKRIGLD KLEECILLQS EMLDLKANPD RVAEGVVIES
RLDRGRGPVA ALLVQKGTLR RGDIVVAGAE WGRVRAVLDD RGRQVKEAGP SMPVEVLGLT
GVPGAGEPFV VVENDARARE ISEFRQRKIK EKEAASQVAA RGTLDQMLAR IQAGVQKEVA
LLIKADVQGS AEAISTTVQK LAHEEVAVRV LNASVGQITE SDIQLAKASD AIIVAFNVRA
TTQARELAQR EGVDIRYYSI IYQVADDVEQ LVKGKVAPKH REKFLGYAEV RQVFNITKTG
KVAGCYVTEG LVKRGCGVRL LRDNVVIHEG ELSQLKRFKD DVKEVARGYE CGLSFAGYND
LREGDMVECY EMEVIPA
