IF2_BIFLS
ID IF2_BIFLS Reviewed; 986 AA.
AC B7GNA3; E8MN46;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=Blon_2198, BLIJ_2272;
OS Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM
OS 1222 / NCTC 11817 / S12).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=391904;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX PubMed=19033196; DOI=10.1073/pnas.0809584105;
RA Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R.,
RA Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P.,
RA Richardson P.M., Mills D.A.;
RT "The genome sequence of Bifidobacterium longum subsp. infantis reveals
RT adaptations for milk utilization within the infant microbiome.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX PubMed=21270894; DOI=10.1038/nature09646;
RA Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T.,
RA Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J.,
RA Morita H., Hattori M., Ohno H.;
RT "Bifidobacteria can protect from enteropathogenic infection through
RT production of acetate.";
RL Nature 469:543-547(2011).
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; CP001095; ACJ53259.1; -; Genomic_DNA.
DR EMBL; AP010889; BAJ69849.1; -; Genomic_DNA.
DR RefSeq; WP_012578457.1; NZ_JDTT01000049.1.
DR AlphaFoldDB; B7GNA3; -.
DR SMR; B7GNA3; -.
DR PRIDE; B7GNA3; -.
DR EnsemblBacteria; ACJ53259; ACJ53259; Blon_2198.
DR KEGG; bln:Blon_2198; -.
DR KEGG; blon:BLIJ_2272; -.
DR PATRIC; fig|391904.8.peg.2273; -.
DR HOGENOM; CLU_006301_9_1_11; -.
DR OMA; QVRPEMI; -.
DR Proteomes; UP000001360; 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..986
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000118751"
FT DOMAIN 479..651
FT /note="tr-type G"
FT REGION 49..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..495
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 513..517
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 538..541
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 592..595
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 628..630
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 80..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 488..495
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 538..542
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 592..595
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 986 AA; 104973 MW; 6C749B62C1635B22 CRC64;
MAKPRVYELA KVLNVDSKTV LEKLKDMGEF VKSASSTIEP PVARRLKAEF AKDNAKGDSK
PASSAQKPAA KPVQQRRPAA PSAPASTSSS APTPAAPARQ ASPASAHQQA PTPGAPTPRP
QGGARPGMPT PGRHGQHDNR ENGRDNREGR ENGRQSRPND RRNNDRRNNQ GRPNNGQPGQ
HQNNRDNASA PRPHAQGGAG ANGGNAASNA IPRPHAQGPR PGNNPFSRKQ GMHTPTPGDI
PRPHPMARPT ADSGRGGRPG RPGQGQGQGR GFRGGRPGQG GQGGPRPGQW GHNRPGQGGG
SQGAGQGGAR GGFRGGQGGG NNFQGGGAPS NGPARGGGRG GRGGAAGAFG RQGGKSSKAR
KNRLAKRHEY EELKAPTIGG VRIPNGNGQT IRLRQGASLA DLAEKINVNQ AALVTVLFHL
GQMATATQSL DEETFQILGG EIGWNIQLVS AEEEDKELLQ QFDINLDEEE LQDDEDLKPR
PPVVTVMGHV DHGKTRLLDT IRKTNVIARE AGGITQRIGA YQVTVNLEGE PRKITFLDTP
GHEAFTAMRA RGAELTDVAI LVVAADDGVM PQTVEAINHA QAAKVPIVVA VNKIDVPGAN
PEKVRGQLTE FGLVPEEYGG DTMFVDISAK QNLHVDKLLE AVLLTADAEL DLRANPDMDA
RGATVEARLD KGRGAVATVL VQQGTLHVGD AIVAGTSYGR VRAMLDENGQ PMEAAGPSTP
VQVLGLTSVP TAGDLFLVAS DDRAARQIAE KRQATERAAQ LAKRRKVVSL EDFKKKFAES
EIDMLNIVIK GDSSGSVEAL EDSLMKIEVS DEVGIQVIHR GVGAITQNDV NLATVDKAVI
IGFNVRPNRQ VADLAEREGV EIKYYSVIYR AIEDIEASLK GMLKPEYEEV VTSHSEIREI
FRSSKFGNIA GVMVQDGEVK RGTKCRILRN GVATVNDLEI SSLRRFKDDV QSVKEGYEAG
INLGTFNDIE LGDIIETFEM QEVERK
