ID A0A095SXV2_9FLAO Unreviewed; 956 AA.
AC A0A095SXV2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=LG45_05910 {ECO:0000313|EMBL:KGD69164.1};
OS Flavobacterium aquatile LMG 4008 = ATCC 11947.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1453498 {ECO:0000313|EMBL:KGD69164.1, ECO:0000313|Proteomes:UP000029554};
RN [1] {ECO:0000313|EMBL:KGD69164.1, ECO:0000313|Proteomes:UP000029554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 4008 {ECO:0000313|EMBL:KGD69164.1,
RC ECO:0000313|Proteomes:UP000029554};
RA Gale A.N., Pipes S.E., Newman J.D.;
RT "Whole Genome Shotgun of Flavobacterium aquatile LMG 4008.";
RL Submitted (SEP-2014) 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:KGD69164.1}.
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DR EMBL; JRHH01000002; KGD69164.1; -; Genomic_DNA.
DR RefSeq; WP_035125249.1; NZ_JRHH01000002.1.
DR AlphaFoldDB; A0A095SXV2; -.
DR STRING; 1453498.LG45_05910; -.
DR eggNOG; COG0532; Bacteria.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000029554; 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 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:UP000029554}.
FT DOMAIN 454..622
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 112..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 68..102
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 123..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 463..470
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 510..514
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 564..567
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 956 AA; 104719 MW; 0FD7A2D1F16E5FFA CRC64;
MSEERNIRIN KVLRELNISL ERAVDYLKDK GIAIDANPNA KISDKEFDIL QNQFAGDKGN
KEASKGVSEE IKKEKEALRL EREKEIEDKR KVEEERQRLE VIKAKAVVSG PKQVGKIELD
PKPGASSKTE EVKAPEAKPQ EVKTPEVKAP EVKIQEVKAP EVKTPEVKAP EVKVEEIKVP
VAEVKAPKVV AIETPKVETK AENTSEVVED ETHTTQYQNL SGPTLTGQKI DLSQFNKPKK
KVETPKINSG SKLNPDPNKN KRKRIPPKPG EARPNTGGNA AGGNTGGPNR PAGGNKFTAN
KPGGGGGFQK GNRPAIVQKV EPTEEEVKNQ IKETLERLQG KGSKSKAAKY RRDKRDTHRQ
RSDDEQKAID EGSKTIKVTE FVTVGEVATM MDVPITKVIG TCMSLGIMVT MNQRLDAETL
SIVADEFGYE VEFITTDLED SIDVVVDREE DLITRAPIVT VMGHVDHGKT SLLDNIRKEN
VIAGESGGIT QHIGAYGVTL DGGQKITFLD TPGHEAFTAM RARGAQVTDI AIIVIAADDD
IMPQTKEAIS HAQAANVPMI FAINKIDKQG ANPEKIKEKL AGMNLLVEDW GGKYQSHDIS
AKSGIGVKEL LEKVLLEAEI LDLKANPNKP AVGTVVEAQL DKGRGYISTI LVQSGTLKIG
DYVLAGKNHG KVKAMHDERG NNITEAGPST PISILGLDGA STAGDKFNVF EDEREAKQIA
AKRTQLMREQ SVRTQRHITL AEIGRRIALG QFKELNIILK GDVDGSVEAL SSEFTKLSTE
EIQINIIHKG VGAITETDVM LASASDAIII GFNVRPAGSA RQLAMKEEID IRNYSIIYDA
INDLKDAMEG MLSPEMKEEI TGTAEIRETF KISKVGTIAG CMVTDGKIFR NSKIRLIREG
VVIFTGELST LKRFKDDVKE VSKGYDCGIQ LKNYNEIEQL DIIEAFQEVE VKKKLK
//
