ID A0A1G6QM27_9BACT Unreviewed; 703 AA.
AC A0A1G6QM27;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=E4650_10035 {ECO:0000313|EMBL:TGG86690.1}, SAMN04488588_2114
GN {ECO:0000313|EMBL:SDC93281.1};
OS Geotoga petraea.
OC Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae; Geotoga.
OX NCBI_TaxID=28234 {ECO:0000313|EMBL:SDC93281.1, ECO:0000313|Proteomes:UP000199322};
RN [1] {ECO:0000313|EMBL:SDC93281.1, ECO:0000313|Proteomes:UP000199322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WG14 {ECO:0000313|EMBL:SDC93281.1,
RC ECO:0000313|Proteomes:UP000199322};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TGG86690.1, ECO:0000313|Proteomes:UP000297288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HO-Geo1 {ECO:0000313|EMBL:TGG86690.1,
RC ECO:0000313|Proteomes:UP000297288};
RA Grouzdev D.S., Semenova E.M., Sokolova D.S., Tourova T.P., Poltaraus A.B.,
RA Nazina T.N.;
RT "Draft genome sequence data and analysis of a Fermenting Bacterium, Geotoga
RT petraea strain HO-Geo1, isolated from heavy-oil petroleum reservoir in
RT Russia.";
RL Submitted (APR-2019) 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}.
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DR EMBL; FMYV01000014; SDC93281.1; -; Genomic_DNA.
DR EMBL; SRME01000010; TGG86690.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6QM27; -.
DR STRING; 28234.SAMN04488588_2114; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000199322; Unassembled WGS sequence.
DR Proteomes; UP000297288; 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; 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.
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:UP000199322}.
FT DOMAIN 193..360
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 50..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 202..209
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 248..252
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 302..305
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 703 AA; 79026 MW; 49A6CD576515B765 CRC64;
MPKIRVYELA KKLDYNSKDL VEILKNELDI DVKSHMSTLE QDTVEAIEDL LAPSKNKEEK
AKKSEKSKKQ EKSKKKKAAP KSEQQNKKEE PVEKEEEKQS IGEINLTPSE LTLDKIAKKL
SVDQNDIIKK AFMEGKMLRP GQELSPTETE EIGLLYETVI NFVEEEKKEE ELDNELVDYW
NKVYEEQKDS LKTRPPVVTV MGHVDHGKTT LLDNIRNTKV AEGEEGGITQ SIGAYQLEYN
DKKITFIDTP GHEAFTEMRA RGAQATDIVV LIIAADDGVM PQTIEAYNHA KDAKVPVIVA
INKIDKPNAN VELTKQQMVA KLNLIPEDWG GDTITVPISA ISKEGIDELL EMISLVSEME
EIKCKPNGQA RAVIIESKLD KFLGPVATVI VKDGILKTGD YFIAGSTYGK VRRMIDDQGR
TIKKALPSTP VQVLGFNEVA DTHSILYVTN SLNQAREISG KKKEKEDLAN QNINKKHVKL
EDFMKMMEGN QKKVLNIILK AGTFGEIEAL KNSINKLQNP DIDIDIVHAG IGTVTTSDIM
LASASDAVVM GFRVKVDNKA KKDAEKEGIQ IKRYDIIFQL IDELKKALQG MLELEEKEEN
TGSGKIKEVF KIKKVGNVAG VIVEDGYVER DGGVRIYRNG SLLQDVKIES LKHYKDEVKR
IEAPQEGGIK FENFDDFNAG DELEFYKNIQ FERQIEFDNS KDR
//
