ID A0A1E8GQZ7_9LACT Unreviewed; 816 AA.
AC A0A1E8GQZ7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-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=BG261_10445 {ECO:0000313|EMBL:OFI50053.1};
OS Floricoccus tropicus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Floricoccus.
OX NCBI_TaxID=1859473 {ECO:0000313|EMBL:OFI50053.1, ECO:0000313|Proteomes:UP000178622};
RN [1] {ECO:0000313|Proteomes:UP000178622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DF1 {ECO:0000313|Proteomes:UP000178622};
RA Chuah L.-O., Yap K.-P., Thong K.L., Liong M.T., Ahmad R., Rusul G.;
RT "Draft genome sequence of a novel species of the family Streptococcaceae
RT isolated from flowers.";
RL Submitted (SEP-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:OFI50053.1}.
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DR EMBL; MKIR01000004; OFI50053.1; -; Genomic_DNA.
DR RefSeq; WP_070791734.1; NZ_MKIR01000004.1.
DR AlphaFoldDB; A0A1E8GQZ7; -.
DR STRING; 1859473.BG261_10445; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000178622; 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; 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; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
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:UP000178622}.
FT DOMAIN 318..487
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 32..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..469
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 48..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 327..334
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 373..377
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 427..430
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 816 AA; 89454 MW; 131EB6DC2E11F060 CRC64;
MSNKKRINEI ARESGLKNKE LIEHAQKLGF DVKTHSSSVD GEQEKKLLAS FKSSNNQAKP
APKKVTNNQS PKQADNNQPK KAAPKQENNR SNNRPVQAQQ GKNSKQNLNN KPQKKQASNQ
NKQVNNQGSQ GQKPANNSNK NNNNRNNQKP NNNQNRQQGN GNNSQARNNN AGGNQNQGQN
RNNNNNRNNN NNNGRNQVRN ARNSNWNSKK KGKRNNQNAA PAVPQRKFHE LPESLVYSDG
MTIADIAKKI KREPAEIVKK LFMMGIMATQ NQSLDSETIE LLLMDYGITP EKKVEVDSAD
IERLFIEDDY LNEDELVERP PVVTIMGHVD HGKTTLLDTL RNSRVTSGEA GGITQHIGAY
QITTEGKKIT FLDTPGHEAF TSMRARGASV TDITILVVAA DDGVMPQTIE AINHSKAAGV
PIIVAINKID KPGANPERVI QELAEHNVMS TSWGGDSEFV QISAKFDKNI DELLETVLLV
AEMLELKADP TVKAIGTVVE ARLDKGKGAI ATLLVQQGTL HQQDPIVVGN TFGRVRAMVN
DLGRREKSAG PSSPVEITGL NDVPQAGDHF AVFDDEKSAR AIGEERAKRA QLLQRQSTNR
VSLENLFDTL KEGEVKSVNV IIKADVQGSA EALAASLQKI DVEGVKVDIV HSAVGAISES
DVSLAEASNA IIIGFNVRPT PLARVQAEQD DVEIRLHSII YKVIEEVETA MKGLLDPEFE
EKVIGEAVVR DTFVVSKVGT IAGFLVTSGT VKRDASVRVI RSGVVIHDGA IASLKHLKDD
VKEVKNGNEG GMMLENFNDV QIDDTFEIYE MVEIKR
//
