IF2_BIFLD
ID IF2_BIFLD Reviewed; 975 AA.
AC B3DQF0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BLD_1743;
OS Bifidobacterium longum (strain DJO10A).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=205913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJO10A;
RX PubMed=18505588; DOI=10.1186/1471-2164-9-247;
RA Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R.,
RA Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V.,
RA Slesarev A.I., Weimer B., O'Sullivan D.J.;
RT "Comparative genomic analysis of the gut bacterium Bifidobacterium longum
RT reveals loci susceptible to deletion during pure culture growth.";
RL BMC Genomics 9:247-247(2008).
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; CP000605; ACD99188.1; -; Genomic_DNA.
DR RefSeq; WP_007055370.1; NC_010816.1.
DR AlphaFoldDB; B3DQF0; -.
DR SMR; B3DQF0; -.
DR EnsemblBacteria; ACD99188; ACD99188; BLD_1743.
DR KEGG; blj:BLD_1743; -.
DR HOGENOM; CLU_006301_9_1_11; -.
DR OMA; QVRPEMI; -.
DR Proteomes; UP000002419; 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 PRINTS; PR00315; ELONGATNFCT.
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.
FT CHAIN 1..975
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093759"
FT DOMAIN 468..640
FT /note="tr-type G"
FT REGION 47..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..484
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 502..506
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 527..530
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 581..584
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 617..619
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 69..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 477..484
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 527..531
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 581..584
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 975 AA; 104024 MW; 4CDFCA04C852D5F3 CRC64;
MAKPRVYELA KVLNVDSKTV LEKLKDMGEF VKSASSTIEP PVARRLKAEF AKDNAKGDSK
PVQQRRPAAP SAPASTSSSA PTPAAPARQA SPASAHQQAP TPGAPTPRPQ GGARPGMPTP
GRHGQNDNRE NGRDNREGRE NGRQSRPNDR RNNDRRNNQG RPNNGQPVQH QNNRGNASAP
RPHAQGGAGA NGGNAASNAI PRPHAQGPRP GNNPFSRKQG MHTPTPGDIP RPHPMARPTA
DNGRGGRPGR PGQGQGQGRG FRGGRPGQGG QGGPRPGQWG HNRPGQGGGS QGAGQGGARG
GFRGGQGGGN NFQGGGAPSN GPARGGGRGG RGGAAGAFGR QGGKSSKARK NRLAKRHEYE
ELKAPTIGGV RIPNGNGQTI RLRQGASLAD LAEKINVNQA ALVTVLFHLG QMATATQSLD
EETFQILGEE IGWNIQLVSA EEEDKELLQQ FDINLDEEEL QDDEDLKPRP PVVTVMGHVD
HGKTRLLDTI RKTNVIAREA GGITQRIGAY QVTVNLEGEP RKITFLDTPG HEAFTAMRAR
GAELTDVAIL VVAADDGVMP QTVEAINHAQ AAKVPIVVAV NKIDVPGANP EKVRGQLTEF
GLVPEEYGGD TMFVDISAKQ NLHVDKLLEA VLLTADAELD LRANPDMDAR GATVEARLDK
GRGAVATVLV QQGTLHVGDA IVAGTSYGRV RAMLDENGQP MEAAGPSTPV QVLGLTSVPT
AGDLFLVASD DRAARQIAEK RQATERAAQL AKRRKVVSLE DFKKKFAESE IDMLNIVIKG
DSSGSVEALE DSLMKIEVSD EVGIQVIHRG VGAITQNDVN LATVDKAVII GFNVRPNRQV
ADLAEREGVE IKYYSVIYRA IEDIEASLKG MLKPEYEEVV TSHSEIREIF RSSKFGNIAG
VMVQDGEVKR GTKCRILRNG VATVNDLEIS SLRRFKDDVQ SVKEGYEAGI NLGTFNDIEL
GDIIETFEMR EVERK
