ID A0A1E7DKJ0_9BACI Unreviewed; 669 AA.
AC A0A1E7DKJ0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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 ORFNames=BA724_10740 {ECO:0000313|EMBL:OES43574.1};
OS Domibacillus iocasae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX NCBI_TaxID=1714016 {ECO:0000313|EMBL:OES43574.1, ECO:0000313|Proteomes:UP000095658};
RN [1] {ECO:0000313|EMBL:OES43574.1, ECO:0000313|Proteomes:UP000095658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29979 {ECO:0000313|EMBL:OES43574.1,
RC ECO:0000313|Proteomes:UP000095658};
RA Verma A., Pal Y., Ojha A.K., Krishnamurthi S.;
RT "Domibacillus iocasae genome sequencing.";
RL Submitted (JUN-2016) 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|ARBA:ARBA00025162, ECO:0000256|HAMAP-
CC Rule:MF_00100, 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: 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:OES43574.1}.
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DR EMBL; MAMP01000024; OES43574.1; -; Genomic_DNA.
DR RefSeq; WP_069939361.1; NZ_MAMP01000024.1.
DR AlphaFoldDB; A0A1E7DKJ0; -.
DR STRING; 1714016.BA724_10740; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000095658; 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; 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; 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; TRANSLATION INITIATION FACTOR IF-2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 1.
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.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00100};
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:UP000095658}.
FT DOMAIN 170..339
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..321
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 179..186
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 225..229
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 279..282
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 669 AA; 72015 MW; E11E48256F384553 CRC64;
MNNKPNNQQS TTNKPAGNRG PAKPKPTGSK PGQQKQGGGQ GGGARSGGAS RPGSRGINGG
PRGKGRSGQR KGAPKQPIPV KKKEIPEKIV FSGSLTVGEL AKKMNVEPSE VIKKLFMLGV
MATINQELDK DAIELVAGEF NVEVEEEILI DKADLETYFE EEEADDNAIE RPAVVTIMGH
VDHGKTTLLD SIRNTKVTEG EAGGITQHIG AYQAETNGKK ITFLDTPGHA AFTTMRARGA
KITDITILVV AADDGVMPQT VEAINHAKAA EVPIIVAVNK IDKPAANPDR VMQELTEHGL
VPEAWGGETI FVPLSAKHGE GIDTLLEMIL LVAEVEELKA DPKRKAMGTV IEAELDKGRG
SVATLLVQNG TLNVGDPIVV GNTFGRVRAM VNDIGRRVKT AGPSTPVEIT GLNEVPLAGD
RFVVFEDEKT ARQIGESRAQ DALQAQRSEK TKVSLDNLFE HMKQGEMKDL NIVLKADVQG
SVEAVAAALQ KIEVEGVNVK IIHTGAGAIT ESDIILASAS NAIVIGFNVR PDVNAKRTAE
VEEVEVRLHR IIYKVIEEIE AAMKGMLDPE FEEKIIGQAE IRQTFKVSKI GTIAGSYVTE
GKITRDSGVR LIRDGIVIFE GEVDALKRFK DDAKEVAQGY ECGITIRGFN DVKEGDIIEA
FIEQEIERK
//