ID A0A1D7XTM1_9FLAO Unreviewed; 862 AA.
AC A0A1D7XTM1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=FORMA_13730 {ECO:0000313|EMBL:AOR26530.1};
OS Formosa sp. Hel3_A1_48.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Formosa.
OX NCBI_TaxID=1336795 {ECO:0000313|EMBL:AOR26530.1, ECO:0000313|Proteomes:UP000094318};
RN [1] {ECO:0000313|EMBL:AOR26530.1, ECO:0000313|Proteomes:UP000094318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hel3_A1_48 {ECO:0000313|EMBL:AOR26530.1,
RC ECO:0000313|Proteomes:UP000094318};
RA Unfried F., Harder J., Teeling H., Hahnke R.L., Markert S., Kappelmann L.,
RA Chafee M.;
RT "Glycan utilization in Formosa spp.";
RL Submitted (SEP-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 -!- 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; CP017259; AOR26530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D7XTM1; -.
DR STRING; 1336795.FORMA_13730; -.
DR KEGG; foh:FORMA_13730; -.
DR PATRIC; fig|1336795.4.peg.1314; -.
DR Proteomes; UP000094318; Chromosome.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000094318}.
FT DOMAIN 361..531
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 85..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 48..84
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 101..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 370..377
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 417..421
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 471..474
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 862 AA; 94856 MW; 7DFE749CE4FAF6A8 CRC64;
MDRAIDFLES KNIEIEKRPT TKISAEVYQL LSGEFQTDAS KKVASKEVGE AKQKEKEALR
QQRELELEEK LKKEEEAKKV IKAKTTFEGP KKVGKIDLNP TKPQPKKEDP KPVIPTKVET
EKPAEAKAAN AVENPTKDVS AEPETESGTV KTQYAKLSGP KSTGQTIDLS QFNKPKKPAA
AKDKNQSNSA DSKKKRKRIS KVGGPNQGQK SRSNRVRNQS KPQTPKVEPT AEEVQKQVRE
TLEKLQGKST KGKGAKYRRD KRDQHRQQTE KDLEQQELES KTLKVTEFVT ANEVATMMDV
SVTEIISACM SLGMMVTMNQ RLDAETLSIV AEEFGYTVDF VTADIDENIE EVEDKAEDLL
ERAPIVTVMG HVDHGKTSLL DYIREENVIA GESGGITQHI GAYGVTLNSG QKIAFLDTPG
HEAFTAMRAR GAQVTDIAII VIAADDNIKP QTKEAISHAQ AAGVPIIFAI NKVDLPTANP
DKIKEGLANM NLMVEDWGGK IQSHDISAKN GDGVQELLEK VLLEAELLEL KANPDKPAVG
TIVEAFLDKG RGYVSTVLVQ AGTLRVGDYV LAGKNSGKVK AMHDERGQEI SEAGPSTPIS
ILGLDGAPQA GDKFTVFKDE REAKQIAAKR TQLQREQSVR TQRHITLDEI GRRIALGDFK
ELNIILKGDV DGSVEALTDS FQKLSTEEIQ VNIIHKAVGA ITESDVLLAS ASDAIIIGFN
VRPMGNARQI AEKEEIDIRM YSIIYDAIND LKDAMEGMLS PEFKEEITGS AEIRETFKIS
KIGTIAGCMV TNGKIYRSSK IRIIREGVVI YTGELASLKR FKDDAKEVSK GYDCGMQIKN
YNDIQLGDVF EAFQEVAVKK KL
//
