ID A0A255TS30_9BACT Unreviewed; 1031 AA.
AC A0A255TS30;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=CIK98_04640 {ECO:0000313|EMBL:OYP67787.1};
OS Prevotella sp. P2-180.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=2024224 {ECO:0000313|EMBL:OYP67787.1, ECO:0000313|Proteomes:UP000216767};
RN [1] {ECO:0000313|EMBL:OYP67787.1, ECO:0000313|Proteomes:UP000216767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P2-180 {ECO:0000313|EMBL:OYP67787.1,
RC ECO:0000313|Proteomes:UP000216767};
RA Accetto T., Nograsek B., Avgustin G.;
RT "Comparative genomics of non-oral Prevotella species.";
RL Submitted (AUG-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}.
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:OYP67787.1}.
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DR EMBL; NPJI01000029; OYP67787.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255TS30; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000216767; 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}.
FT DOMAIN 530..700
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 100..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 539..546
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 586..590
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 640..643
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1031 AA; 113417 MW; F6A45972198E2A5F CRC64;
MGIRLNKVLT ELNIGLQTAV DFLRNKKSLG EIAEDANLST KISDEQYNAL VSQFKGDKDI
KNEAEKLAKK GKERKAEKKI SNTKADDLVK KVQKYTPLGK IDLDSIGKPA KASSDAIETK
PEIKTTAESL NKGNTTERNE VDKSQQININ KQNNDNTANN EKNAPKASDS NSTEKADNID
NVKKAETEMT TDNNNIILPE TKQKAIESNE NVKSEKINQN GKDAMQNDMG NSQSNQKNTK
VDNNSNQNSN QNRQNGKSAA SIDNSQNKQT QEARNDNKIF TLRSEKKLAP KVNVLGKIDL
DALNQSTRPK KKTKEERRKE REEKAIHNGE RKKRVRINNE RVDIEAAANQ GGSNKKKKNR
GGNNQGNANN QGNANNQQGG GGKNKNKAKN KPQKPIEVNE EDVARQVKET LARLTNKNQN
KKGAKYRREK REAVQERLNE ELMEQAAESK TLKLTEFVTV SELATMMNVP VNQVIGTCMS
IGIMVSINQR LDAETINIVA DEFGFKTEYV SAEVSEAVSE EVDDENDLVP RAPIVTVMGH
VDHGKTSLLD HIRKSNVIAG EAGGITQHIG AYNVTLGDGR QITFLDTPGH EAFTAMRARG
AQVTDIAIII IAADDSVMPT TKEAIAHAQA ANVPMVFAIN KIDKPGANPD KIREDLANMN
LLVEEWGGKY QCQEISAKKG IGVQELLEKV LLEAEMLDLK ANPNRKATGS VIESSLDKGR
GYVSTVLVSN GTLKVGDIVI AGTSHGRIKA MFNERNQRIE KALPSEPATI LGLNGAPQAG
DSFHIMDTEQ EAKEIANKRT QLQREQSLRT ATTLSLEEIA HRVALGEFHE LNLVVKADTQ
GSVEALSDSF IKMSTEKVQV NVILKAVGQI SENDVMLAST AKGMIVGFQV RPSVEAKRLA
EREGVEINTY SVIYDAIDDI HSAMEGMLEK VKKEVATGQV EVREVYKISK VGTVAGAFVT
EGKVHRTDKA RLIRDGIVVH TGDINALKRY KDDVKEVAAN FECGISLVNF NDIQQGDIIE
TFTEIEVEQK L
//
