ID A0A2A4Q370_9BACT Unreviewed; 496 AA.
AC A0A2A4Q370;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|RuleBase:RU000644};
GN Name=infB {ECO:0000313|EMBL:PCH91020.1};
GN ORFNames=COB87_00075 {ECO:0000313|EMBL:PCH91020.1};
OS Candidatus Wolfebacteria bacterium.
OC Bacteria; Candidatus Wolfebacteria.
OX NCBI_TaxID=2030812 {ECO:0000313|EMBL:PCH91020.1};
RN [1] {ECO:0000313|EMBL:PCH91020.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NORP156 {ECO:0000313|EMBL:PCH91020.1};
RX PubMed=29099490; DOI=.1038/ismej.2017.187;
RA Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT "A dynamic microbial community with high functional redundancy inhabits the
RT cold, oxic subseafloor aquifer.";
RL ISME J. 12:1-16(2018).
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|RuleBase:RU000644}.
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|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:PCH91020.1}.
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DR EMBL; NVRX01000001; PCH91020.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4Q370; -.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd01887; IF2_eIF5B; 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 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 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 GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000256|RuleBase:RU000644};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU000644}.
FT DOMAIN 7..180
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 496 AA; 53336 MW; CB1F2509B43A27B2 CRC64;
MSNNTTTRPP VVAVMGHIDH GKSSLLDYIR KENTVDGEAG GITQHVSAYE VIHKTKDGEK
KITFLDTPGH EAFRAMRASG ADIADIAILI VAGDDGVKPQ TIEAHKAIKD AGIPFVVAIT
KMDTNGADLE KVKTSLLENE IYLEGLGGDV PFAPISSKTG DGVPELLDLI LLAAELEELT
GDEKASASGV VLEATKDKKR GDSATLIIKN GTLSIGSFIV SKNSVSPIRF IEDFKGDRID
TATFSSPVRI VGFNTLPEVG APFSVVAKKK EAEKLAKSYV GEKVEISYEP IKKREGAILP
LIIKTDVVGS LPAIEHELAK ISHENITIKV VTSGVGAINE GDIKTAVAAP EGVVVAFHTG
ISTSVASLAE RKGIEAKNFD IIYNLAEYVK ETLIARAPKI QKEEILGEAK IIRLFNKVGT
KQVFGAKVKK GEMRLNSTVR ILRRNVLLGE GKLTNLQSMR VDVDSVPVDT EFGGELDSKI
EFVEGDYIEA YHIVES
//
