ID A0A1T5LHK9_9BACT Unreviewed; 975 AA.
AC A0A1T5LHK9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=SAMN05660236_3258 {ECO:0000313|EMBL:SKC75506.1};
OS Ohtaekwangia koreensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC Ohtaekwangia.
OX NCBI_TaxID=688867 {ECO:0000313|EMBL:SKC75506.1, ECO:0000313|Proteomes:UP000190961};
RN [1] {ECO:0000313|EMBL:SKC75506.1, ECO:0000313|Proteomes:UP000190961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25262 {ECO:0000313|EMBL:SKC75506.1,
RC ECO:0000313|Proteomes:UP000190961};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Abolishes the inhibitory effect of tetracyclin on protein
CC synthesis by a non-covalent modification of the ribosomes.
CC {ECO:0000256|ARBA:ARBA00003987}.
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; FUZU01000002; SKC75506.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5LHK9; -.
DR STRING; 688867.SAMN05660236_3258; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000190961; 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; 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.
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:UP000190961}.
FT DOMAIN 474..644
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 240..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 483..490
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 530..534
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 584..587
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 975 AA; 106609 MW; 4FB96F480A9144D2 CRC64;
MAEEKLIRLS QAARKLNVGH NTILDFLGKK GFEVENNPNA KLTPEQFNLL SKEFASSATD
KLEASGLHIG AKHVDNLVLE SEKELAKKRV EEEERIMIKN LGSKEVKAKD EPKPADKVER
EKPKLEGIKV IGKIDLEKKP VAKEEVVEEP PVVEKPVVEK PVPVIEKIEV PEVKEVIPEP
KEQKEIKEIP EVKEVPKEVI KETPPPVKEP VVVVPPKVVE QKPPVVAEKA EPEMELIKAK
ADRLKGLKVV DKIELPVDKK KDSPVASSDT KDDRKGKRPR KRIPTADDQQ RGPGQQQQGG
GQQGGGQQGQ GGQRPNPQQR PNQQHGQQRR GPHAPRVQKE EPTEKEIQDQ IRATLAKLSG
GGKKTSGSKY RREKRQANSD AQEQQMLQEQ EASKTLRVTE FISANDLASL MDVSVNDVIS
TCLSLGMFVS INQRLDAEAI TVITDEFGYA VQFTSAEEEL EVEEEQGNDV NLQHRAPIVT
IMGHVDHGKT SLLDYIRNTK VTASEAGGIT QHIGAYDVTT KSGNKIAFLD TPGHEAFTAM
RARGAKLTDI AIIVVAADDD VMPQTREAIN HAQVAGVPIV IAINKIDKPS ANPDKIREAL
SKNNILVEEW GGKYQSQEIS AKTGKGIDDL LEKVLLEAEI LNLKANPDKN ASGSVIEASL
DKGRGYVATI MVQTGTLKVG DIVLAGAHYG RVKAMFDDTG KKVNEAGPST PVVLLGLDGA
PQAGEKVTVM ETDREARELA GKRSQLLREQ SIRTKKHITL DEIGRRLAIG SFKQLNVIVK
GDVDGSVEAL SDSLLKLSTP EIQVAIIHRG VGQISESDVL LASASDAIIL GFQVRPSNAA
KRVAENEEIE IRLYSIIYDA INDVRAAMEG MLAPETEEVI VGNAEVREVF KISKIGTIAG
CMITDGSVKR SNPIRLIRDG IVVYAGKLGS LKRHKDDASE VRSGFDCGIG IDGFNDMQVG
DVIESYEQRE VKRTL
//
