IF2_BIFLO
ID IF2_BIFLO Reviewed; 954 AA.
AC Q8G3Y5;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BL1616;
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=206672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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; AE014295; AAN25404.1; -; Genomic_DNA.
DR RefSeq; NP_696768.1; NC_004307.2.
DR RefSeq; WP_011068747.1; NC_004307.2.
DR AlphaFoldDB; Q8G3Y5; -.
DR SMR; Q8G3Y5; -.
DR STRING; 206672.BL1616; -.
DR EnsemblBacteria; AAN25404; AAN25404; BL1616.
DR KEGG; blo:BL1616; -.
DR PATRIC; fig|206672.9.peg.1671; -.
DR HOGENOM; CLU_006301_9_3_11; -.
DR OMA; QVRPEMI; -.
DR PhylomeDB; Q8G3Y5; -.
DR Proteomes; UP000000439; 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..954
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137172"
FT DOMAIN 447..619
FT /note="tr-type G"
FT REGION 47..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..463
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 481..485
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 506..509
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 560..563
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 596..598
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 456..463
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 506..510
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 560..563
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 954 AA; 102184 MW; 980F43ABAB599C89 CRC64;
MAKPRVYELA KVLNVDSKTV LEKLKDMGEF VKSASSTIEP PVARRLKAEF AKDNAKGDSK
PVQQRRPAAP SAPASTSSSA PTPAAPARQA SPASAHQQAP TPGAPTPRPQ GGARPGMPTP
GRHGQNDNRE NGRDNREGRE NGRQSRPNDR RNNDRRNNQG RPNNSQPVQH QNNRGNASAP
RPHAQGPRPG NNPFSRKQGM HTPTPGDIPR PHPMARPTAD NGRGGRPGRP GQGQGQGRGF
RGGRPGQGGQ GGPRPGQWGH NRPGQGGGSQ GAGQGGARGG FRGGQGGGNN FQGGGAPSNG
PARGGGRGGR GGAAGAFGRQ GGKSSKARKN RLAKRHEYEE LKAPTIGGVR IPNGNGQTIR
LRQGASLADL AEKINVNQAA LVTVLFHLGQ MATATQSLDE ETFQILGEEI GWNIQLVSAE
EEDKELLQQF DINLDEEELQ DDEDLKPRPP VVTVMGHVDH GKTRLLDTIR KTNVIAREAG
GITQRIGAYQ VTVNLEGEPR KITFLDTPGH EAFTAMRARG AELTDVAILV VAADDGVMPQ
TVEAINHAQA AKVPIVVAVN KIDVPGANPE KVRGQLTEFG LVPEEYGGDT MFVDISAKQN
LHVDKLLEAV LLTADAELDL RANPDMDARG ATVEARLDKG RGAVATVLVQ QGTLHVGDAI
VAGTSYGRVR AMLDENGQPM EAAGPSTPVQ VLGLTSVPTA GDLFLVASDD RAARQIAEKR
QATERAAQLA KRRKVVSLED FKKKFAESEI DMLNIVIKGD SSGSVEALED SLMKIEVSDE
VGIQVIHRGV GAITQNDVNL ATVDKAVIIG FNVRPNRQVA DLAEREGVEI KYYSVIYRAI
EDIEASLKGM LKPEYEEVVT SHSEIREIFR SSKFGNIAGV MVQDGEVKRG TKCRILRNGV
ATVNDLEISS LRRFKDDVQS VKEGYEAGIN LGTFNDIELG DIIETFEMRE VERK
