IF2_BIFA0
ID IF2_BIFA0 Reviewed; 944 AA.
AC B8DW43;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BLA_0392;
OS Bifidobacterium animalis subsp. lactis (strain AD011).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=442563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD011;
RX PubMed=19011029; DOI=10.1128/jb.01515-08;
RA Kim J.F., Jeong H., Yu D.S., Choi S.-H., Hur C.-G., Park M.-S., Yoon S.H.,
RA Kim D.-W., Ji G.E., Park H.-S., Oh T.K.;
RT "Genome sequence of the probiotic bacterium Bifidobacterium animalis subsp.
RT lactis AD011.";
RL J. Bacteriol. 191:678-679(2009).
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; CP001213; ACL28694.1; -; Genomic_DNA.
DR RefSeq; WP_004268627.1; NC_011835.1.
DR AlphaFoldDB; B8DW43; -.
DR SMR; B8DW43; -.
DR STRING; 442563.BLA_0392; -.
DR PRIDE; B8DW43; -.
DR EnsemblBacteria; ACL28694; ACL28694; BLA_0392.
DR GeneID; 66532776; -.
DR KEGG; bla:BLA_0392; -.
DR HOGENOM; CLU_006301_9_3_11; -.
DR OMA; QVRPEMI; -.
DR Proteomes; UP000002456; 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; Reference proteome.
FT CHAIN 1..944
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000118750"
FT DOMAIN 437..609
FT /note="tr-type G"
FT REGION 48..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..453
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 471..475
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 496..499
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 550..553
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 586..588
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 98..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 446..453
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 496..500
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 550..553
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 944 AA; 100016 MW; 2DA00BCD8AF1DA9A CRC64;
MAKARVYELA KELGVDSKTV LEKLKDMGEF VKSASSTVEA PVVRRLKAAF PKDGGNDSRP
SAKKSSTPKS GAPAAAKPAA TPAAVAGATP ATAAPSAPKP GQRSNTSAKP GAHNTRRNEQ
TPRPGQNGGQ RGATARPHAP GKPGANAGGT RNGGKAAPTP HAPQHGGNRG GSNNAPKPGA
NAAQHAPRPG NNPFSRKQGM HTPTPGDIPR PHPMARPTVN NNERRGGGNG RPGQRGGFRP
RPGQGGSGAP KPGSWGQHRQ GAGSGGGRPG GNRFGGGNGG NNFQNNGPSN GPSRGGGRGR
GGAAGAFGRQ GGKSSKARKN RLAKRHEYEE LKAPVIGGVR IPTGNGQTIR LRQGASLADL
AEKINVNPAA LVTVLFHLGE MATATQSLDE STFQILGEEI GWNIKIVSAE EEDKELLQQF
DIDLESEELQ EEADLKPRPP VVTVMGHVDH GKTRLLDTIR RTNVVAREAG GITQRIGAYQ
VTVDLEGEER KITFLDTPGH EAFTAMRARG AELTDIAILV VAADDGVMPQ TVEAINHAQS
AHVPIVVAVN KIDVPGANPE KVRGQLTEFG LVPEEYGGST MFVDISAKQG TNVDKLLEAV
LLTADAELDL RANPDMDARG ATVEARLDKG RGAVATVLVQ SGTLHIGDSI VAGTSYGRVR
AMLDENGKHM KEALPSTPVQ VLGLTSVPTA GDLFLVAPDD RAARQIAEKR QATERAAQLA
KRRKVVSLEE FKKKFAESEI DMLNIVIKGD SSGSVEALEG SLMKIEVSDE VGIQVIHRGV
GAITQNDVNL ASVDKAVIIG FNVRPNRQVA DLAEREGVEI KYYSVIYKAI EDIEASLKGM
LKPEYEEVTT SHSEIREIFR SSKFGNIAGV MVLDGEVKRG TKARILRDGV TTFNDLEISS
LRRFKDDVKS VTEGYEAGIN LGNFNDIEIG DVIETFEMRE IERK
