ID A0A086ZIP6_9BIFI Unreviewed; 939 AA.
AC A0A086ZIP6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000256|HAMAP-Rule:MF_00100,
GN ECO:0000313|EMBL:NMF02252.1};
GN ORFNames=BBOU_1488 {ECO:0000313|EMBL:KFI46396.1}, HF843_03505
GN {ECO:0000313|EMBL:NMF02252.1};
OS Bifidobacterium boum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=78343 {ECO:0000313|EMBL:KFI46396.1, ECO:0000313|Proteomes:UP000029093};
RN [1] {ECO:0000313|EMBL:KFI46396.1, ECO:0000313|Proteomes:UP000029093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 10736 {ECO:0000313|EMBL:KFI46396.1,
RC ECO:0000313|Proteomes:UP000029093};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:NMF02252.1, ECO:0000313|Proteomes:UP000583419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCA-130-P53-4B {ECO:0000313|EMBL:NMF02252.1,
RC ECO:0000313|Proteomes:UP000583419};
RA Hitch T.C.A., Wylensek D., Clavel T.;
RL Submitted (APR-2020) 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:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|ARBA:ARBA00007733, ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFI46396.1}.
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DR EMBL; JGYQ01000016; KFI46396.1; -; Genomic_DNA.
DR EMBL; JABAGJ010000004; NMF02252.1; -; Genomic_DNA.
DR RefSeq; WP_026502381.1; NZ_JGYQ01000016.1.
DR AlphaFoldDB; A0A086ZIP6; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000029093; Unassembled WGS sequence.
DR Proteomes; UP000583419; Unassembled WGS sequence.
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; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 1.10.10.2480; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR004161; EFTu-like_2.
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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00100};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00100}; Hydrolase {ECO:0000313|EMBL:KFI46396.1};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00100}; Reference proteome {ECO:0000313|Proteomes:UP000029093}.
FT DOMAIN 432..604
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 49..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 441..448
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 491..495
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 545..548
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 939 AA; 100841 MW; B61B5A9F5EDE8995 CRC64;
MAKQRVYELA KELGVDSKTV LEKLKDMGEF VKSASSTVEA PVVRRLKASF PKADAQNKPS
EKKQGAAKAA PRPGQHTEHS QESQAKHAEH RTSVKPGPAH MQVPKPGAPH PGPHAAQRSQ
QGGRPDRPQR RDDRRDGRNA RSERGEQPRP GQHTNTRRSN APRPGAGNTP HAPRNAQGAP
QQGRTGAPHA ATPGPRPGNN PFSRKQGMHV PTPGDIPRPH PMARPTVEGG RGGRGRGGRN
GFGNGRAGAK PGQWGQHRPG QNGGNRSAGA GNHFGGGFQN GGGNAGPSRP GGRGRGGAAG
AFGRQGGKSS KARKNRLAKR HEYQEMKAPV IAGVRIPAGN GQTVRLRQGA SLADLAEKIN
VNPAALVTVL FHLGEMATAT QSLDEATFQI LGEEIGWNIK IVSAEEEDKE LLQQFDIDLD
SEELQDDENL KPRPPVVTVM GHVDHGKTRL LDTIRKTNVV AREAGGITQR IGAYQVTVKL
DGESRKITFL DTPGHEAFTA MRARGAELTD IAILVVAADD GVMPQTVEAI NHAQAAHVPI
VVAVNKIDKP GANPERVRGQ LTEFGLVPEE YGGNTMFVDI SAKQGTNVDK LLEAVLLTAD
AELDLRANPD MDARGATVEA RLDKGRGAVA TVLVQSGTLH VGDAIVAGTS YGRVRAMLDE
NGNHMKAAGP STPVQVLGLT SVPTAGDLFL VAPDDRAARQ IAEKRQATER AAQLAKRRKV
VSLESLKEQF AKSEVDMLNI VIKGDSSGSV EALEDSLMKI DVSEEVGIQV IHRGVGAITQ
NDVNLASVDK AVIIGFNVRP NRQVADLAER EGVEIKYYSI IYKAIEDVEA SLKGMLKPEY
EEVVTSHSEI REIFRSSKFG NIAGVMVQDG EVKRGTKCRI LRNGVATVND LEISSLRRFK
DDVQSVKEGY EAGINLGTFN DIEIGDIIET FEMREIERK
//
