IF2_ALKHC
ID IF2_ALKHC Reviewed; 730 AA.
AC Q9KA77;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BH2413;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB06132.1; -; Genomic_DNA.
DR PIR; E83951; E83951.
DR RefSeq; WP_010898566.1; NC_002570.2.
DR AlphaFoldDB; Q9KA77; -.
DR SMR; Q9KA77; -.
DR STRING; 272558.10175033; -.
DR EnsemblBacteria; BAB06132; BAB06132; BAB06132.
DR KEGG; bha:BH2413; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001258; 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..730
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137169"
FT DOMAIN 231..400
FT /note="tr-type G"
FT REGION 48..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..247
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 265..269
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 286..289
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 340..343
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 376..378
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 62..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..131
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 240..247
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 286..290
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 340..343
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 730 AA; 79994 MW; 016CC32FC226553B CRC64;
MRKMRIYEYA KEKNLSSKEV IEKLKGLNVH VSNHMSVIDE KTITLLEGNG NQKQGGSGKP
EQQKKAGEKK PAQDHGQRKP NTAPAKANNQ HDRSQGSDQQ KGKAQDGGQK PKHKGNKNKK
QHQKNNNNKR NQRGRGRQPE MNKAKPLPEK VTFSGSLTVG ELAEKLNKEP SELIKKLMFL
GVMATINQEL DKDSIELICE DYGVEVEEEV IIDETDIESY VVEDDPSLLK ERPPVVTIMG
HVDHGKTTLL DSIRNTKVTE GEAGGITQHI GAYQVTVEGK KITFLDTPGH AAFTTMRARG
AQVTDITILV VAADDGVMPQ TKEAISHAKA AGVPIIVAVN KMDKETANPD RVMQELTEYE
LVPEAWGGET IFVNVSALTG TGIDELLEMV LLVAEVEELK ANPDRLARGT VIEAELDKGR
GPVATLLVQS GTLKVGDPIV VGSTFGRVRA MVNDEGRRVK AVGPSTPVEI TGLNDVPQAG
DQFQAFADEK KARSIGEARA TRQKEEERAE TSKVSLDDLF NQIQQGEVKE INVIIKADVQ
GSVEAMRGSL EKIDVEGVKI NIIHTGVGAI TESDIILAAA SNAIVIGFNV RPDGGAKRTA
EQEKVDIRLH RVIYNAIEEI EAAMKGMLDP EYEEKIIGQV EVRTTFKVSR IGTIAGSYVT
EGKIVRDATV RLIRDGVVIY EGSINALKRF KDDVKEVAQG YECGITLENF NDIKEGDIIE
AYVMEEIERT
