ID A0A1G8H4U6_9FLAO Unreviewed; 991 AA.
AC A0A1G8H4U6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=SAMN05421846_103252 {ECO:0000313|EMBL:SDI01589.1};
OS Chryseobacterium taeanense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=311334 {ECO:0000313|EMBL:SDI01589.1, ECO:0000313|Proteomes:UP000198869};
RN [1] {ECO:0000313|Proteomes:UP000198869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17071 {ECO:0000313|Proteomes:UP000198869};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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 ECO:0000256|RuleBase:RU000645}.
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; FNDW01000003; SDI01589.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8H4U6; -.
DR STRING; 311334.SAMN05421846_103252; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000198869; 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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 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|ARBA:ARBA00022490, 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 487..657
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 96..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 496..503
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 543..547
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 597..600
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 991 AA; 108858 MW; 5DF57F0A8D063B24 CRC64;
MPKIRLNKAV KEFNISMSRL VEFLQSKGIE VESNPNAQLE EAAYSALEAE FAKDGEQRKA
SHEVVITKVP EEKLEIEEKK TPEVIRAKAN KPETKILGKI DLEPKKPEVE ETPAPKPEPV
VEEKKEEAAP EVKATPEKQE FKVLDKIDLS QIESRNRPVK KDKPKTEDKK EETKPVEKTA
QAVKETPKPA VEVPSKPVEE KKETPKQEEE SQEPQKIETV YQKLDGPKIV GEKIDLTQFA
PKQGAGAKKK RKRIEKPGGQ NQQGGNNNQQ GGQNRPQGQG GQGGNRPQGQ GGNRFGNNNQ
GGQNRPQGQG GQGGNRFGNN NQGNRPPGQG NRPPGQGGNR FGNNRPGQRT MPVELTDEQV
KNQIKETLEK LTNKGGKSKS AKHRKDKRNF RREQDERQQE IDAADRTLKV TEFITVGELA
SLMNVSPTEV ISACFSLGVM VTMNQRLEAD TLLLVADEFG YKIEFSDADL EETETEDEID
NEENLVSRAP VVTVMGHVDH GKTSLLDYIR KTNVIAGESG GITQHIGAYN VKLENGQRIT
FLDTPGHEAF TAMRARGAQI TDIAIIVIAA DDDVMPQTKE AIAHAQAAQV PMIIAINKVD
KPNANPDNIR QQLSGLNPPV LVEEWGGNVQ AQEISAKMGN NIDLLLEKVL LQAEILELKA
NPARSANGVV IEASLDKGRG YVATMLVQSG TLKVGDYVVA GKNHGKVKAL LDERGKNLAE
AGPSIPATIL GLDGAPTAGD KFRVYADESE GKAIANKREQ LQRELSIRTK KHTTLEELGR
RIALGEFKEL NIILKGDVDG SVEALSDQLQ RLSTEEISVK ILHSGVGQIT ESDINLAAAS
DAIIIGFNVR AGANAKDLAD REEIEIRTYS VIYKAIDEVK EAMEGMLSPE IQEQVIGNVE
IREVFKISKV GTIAGCMVLT GKVTRQSKIR LLRDGIVKFE GELESLKRFK DDVKEVTKGY
ECGLNLKGYN DIEIGDILEV YEEVAVKKKL K
//
