ID A0A0L8V8G6_9BACT Unreviewed; 999 AA.
AC A0A0L8V8G6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=NC99_24010 {ECO:0000313|EMBL:KOH44741.1};
OS Sunxiuqinia dokdonensis.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Sunxiuqinia.
OX NCBI_TaxID=1409788 {ECO:0000313|EMBL:KOH44741.1, ECO:0000313|Proteomes:UP000036958};
RN [1] {ECO:0000313|Proteomes:UP000036958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK {ECO:0000313|Proteomes:UP000036958};
RA Ahn S., Kim B.-C.;
RT "Genome sequencing of Sunxiuqinia dokdonensis strain SK.";
RL Submitted (JUL-2015) 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}.
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:KOH44741.1}.
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DR EMBL; LGIA01000153; KOH44741.1; -; Genomic_DNA.
DR RefSeq; WP_053183610.1; NZ_LGIA01000153.1.
DR AlphaFoldDB; A0A0L8V8G6; -.
DR STRING; 1409788.NC99_24010; -.
DR PATRIC; fig|1409788.3.peg.2480; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000036958; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000036958}.
FT DOMAIN 498..668
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 70..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..104
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 507..514
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 554..558
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 608..611
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 999 AA; 111064 MW; D0A44664CA316723 CRC64;
MAIGKKSTRL SKVAREFNVG TNTIVEFLHK KGFDIDANPN SKISEDAYHM LEKEYKSDIT
LKKESEKINL MSHRSKNESI SLENANADTE EDVDQDDEEE EVEEVRIKDM NPPKKETPKA
KPEPKPQPEE EKEKLPEVDQ PKVLGKIDLD SIQPKKREGK PTVIKKGDQK QEEPKAAKPK
EEEKQIETPK AEVSKPVEPK PVPEEEKPAE VEKQTEPIEE VQTNIPKVDE VKVVGRIDLS
SINQKTRPTK KTKKQKEDER KERDKQKRQT SQEQGRDRDK DIKTNVEKLS GPNVVGKIDI
KKKKPVASST DTSAQNAKKK RRRIQKDSDS RINVVKPGQG QPQGQGQRGR MQQQGGKGKR
KIIKKEVSEE DVQKQIKDTL ARLTSGKQKS KGSKYRRDKR QAASDKASAA HERESAEQYV
LKVTEFVSVS ELATMMDVSV TEVISSCMSL GLFVSINQRL DAETMSIVAE EFGYEVEFVS
ADILDGVDDD DEPEQVHPRA PIVTVMGHVD HGKTSLLDHI RSANVIAGEA GGITQHIGAY
HVSLADGRMI TFLDTPGHEA FTAMRARGAQ VTDIAIIIVA ADDDIMPQTK EAINHAQAAG
VPIVFAINKI DKPNANPDKI KEGLANLNFL VEEWGGKYQS QDISAKNGVN IDELLEKVLL
EAEMLELKGN KDRRATGTIV ESSLDRGRGY VATVLVQNGT LHQGDIMLAG KYYGHIKAMF
NERNQRIESA GPSEPVIILG LDGAPQAGDK FNVFENEREA RQIANKREQL AREQGLRTQK
HITLDEIGRR IAIGNFQELN LIVKGDVDGS IEALSDALIK LSTDEIQVNV IHKAVGAISE
SDVMLATASD AIVVGFQVRP SMQARKLAEK EEVDIRLYSI IYDAINEIKS AMEGMLSPEI
KEEILGTAEV MEAFKITKVG TIAGCIVRDG KIHRNNKVRL IRDGIVIYTG TLGSLKRFKD
DVKEVQKGYE CGLNIDGYND VKEGDMIEAF HEIEVAKSL
//
