IF2_BIFAA
ID IF2_BIFAA Reviewed; 931 AA.
AC A1A0A2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BAD_0354;
OS Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS E194a).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=367928;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RA Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA Tanaka K., Watanabe K.;
RT "Bifidobacterium adolescentis complete genome sequence.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; AP009256; BAF39135.1; -; Genomic_DNA.
DR RefSeq; WP_011742835.1; NC_008618.1.
DR AlphaFoldDB; A1A0A2; -.
DR SMR; A1A0A2; -.
DR STRING; 1680.BADO_0361; -.
DR EnsemblBacteria; BAF39135; BAF39135; BAD_0354.
DR GeneID; 56674427; -.
DR KEGG; bad:BAD_0354; -.
DR HOGENOM; CLU_006301_9_1_11; -.
DR OMA; QVRPEMI; -.
DR Proteomes; UP000008702; 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..931
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008203"
FT DOMAIN 424..596
FT /note="tr-type G"
FT REGION 32..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..440
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 458..462
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 483..486
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 537..540
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 573..575
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 81..95
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 433..440
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 483..487
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 537..540
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 931 AA; 99003 MW; A6EA447B6C60EE5B CRC64;
MPKARVYELA KELGVDSKTV LSKLEAMGEF VKSASSTVEP PVARKLRNAF ASSGQGNASD
SKKPGHTAKK PAEPASHSMP KPAAPSAPKP AAPAAPKPRH AASKSDAPKP GHRAPRPGES
RQHGNRPNGN APRPQGGDRR QSGRPTAVPG ARPQHGNAPQ GGNNANGAKP HTPGPRPGNN
PFSRKQGMHT PTPGDIPRPH PMNRPSVNNG EGRRGGRPGQ GGGQRGGFRG RPGQGGAKPG
QWGQHRPGQG GGQRPAGGGN RFGGNGGGFQ GGNSAPSNGP ARGGRGRGGA AGAFGRQGGK
SSKARKNRLA KRQEFQEMKA PVIGGVRIPT GNGQEVRLRQ GASLADLAEK INVNPAALVT
VLFHLGEMAT ATQSLDEATF QILGEEIGWN IKIVSAEEED KELLQQFDIN LDEEELQEDG
DLKPRPPVVT VMGHVDHGKT RLLDTIRRTN VIEGEAGGIT QRIGAYQVTV NLEGEPRKIT
FLDTPGHEAF TAMRARGAEL TDVAILVVAA DDGVMPQTVE AINHAQAAHV PIVVAVNKID
KPGANPDKVR GQLTEYGLVP EEYGGNTMFV DISAKQGTNV DKLLEAVLLT ADAELDLRAN
PDMDARGATV EARLDKGRGA VATVLVQSGT LHIGDAIVAG TSYGRVRAML DENGNHMQEA
GPSTPVQVLG LTSVPTAGDL FLVASDDRTA RQIAEKRQAT ERAAQLAKRR KVVSLESLKE
QFAKSEVDML NIVIKGDSSG SVEALEDSLM KIEVSDEVGI QVIHRGVGAI TQNDVNLATV
DKAVIIGFNV RPNRQVADLA EREGVEIKYY SIIYKAIEDI EASLKGMLKP EYEEVVTSHS
EIREIFRSSK FGNIAGVMVQ DGEVKRGTKC RILRNGIATV NDLEISSLRR FKDDVTSVKE
GYEAGINLGT FNDIEIGDII ETFEMQEIER K
