ID A0A1T5BZC5_9BACT Unreviewed; 989 AA.
AC A0A1T5BZC5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=SAMN03080601_00699 {ECO:0000313|EMBL:SKB52491.1};
OS Alkalitalea saponilacus.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC Alkalitalea.
OX NCBI_TaxID=889453 {ECO:0000313|EMBL:SKB52491.1, ECO:0000313|Proteomes:UP000191055};
RN [1] {ECO:0000313|EMBL:SKB52491.1, ECO:0000313|Proteomes:UP000191055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24412 {ECO:0000313|EMBL:SKB52491.1,
RC ECO:0000313|Proteomes:UP000191055};
RA Peterson S.W.;
RL Submitted (FEB-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 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; FUYV01000002; SKB52491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5BZC5; -.
DR STRING; 889453.SAMN03080601_00699; -.
DR KEGG; asx:CDL62_10460; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000191055; 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}; Reference proteome {ECO:0000313|Proteomes:UP000191055}.
FT DOMAIN 488..658
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 76..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 497..504
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 544..548
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 598..601
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 989 AA; 109355 MW; D86FFC00E0C7881A CRC64;
MAVGQRLSKV AKELNVGTST IVDFLQKKGV EIDVNPNTKV SPEIFELLKN EFKQDLSVKK
ASEELIERKL KEKKETISID KVKKDEEISD EEDDDIEEVL KPQVRKNVDV KVVGKIDLEK
KPAPKPQEKP VPPKEEPKPV AEKPTPKKEE APKPKETSKP EPEHIPVSVK KPVEEPRVVG
KIDLDKKPKA KEAERKKEEK PKEQAQPVKE ERPATDIKKE VPVKAEQPAK EIKVETPAPK
QEEPKAKATS QESKDSDFVP TKIKKLTGPT VVGKIELPKD TRNGDNRDDK KGRKKKRKRI
KKEKERVNIN AAGEKTTGGQ GPKTGTPQQQ GDKSAERKAA ARKKAPKVKK RPARPEVSEE
DVAKQIKDTL ARLTSKGKSK ASRHRRDKRD MASQRHMAEQ ERMDEEKKIL KVTEFVTANE
LANMMDVQVN QIIASCMSLG LFVSINQRLD AETIALVAEE FGYKVEFVSV DLAESISEYE
DTPEDLQDRP AIVTVMGHVD HGKTSLLDYI RKSDVTAGEA GGITQHIGAY GVKLDSGKKI
TFLDTPGHEA FTAMRARGAQ VTDIAIIIIA ANDNVMPQTI EAINHASAAG VPIVFAISKI
DVPGANPDKV RESLANMNYL VEDWGGKYQC QEVSAKHGTN VKQLLEKVLL EAEMLELKAN
PVKPAVGSVI ESTLDKGRGF VATLLVQAGT LKVGDLILAG SYYGHVKAMF NERNQKIEEA
GPSDPVLILG LNGAPQAGEK FNVMESEKET KDIATKRLQL QREQGMRAQK HITLDEIGRR
IAIGNFQELN LIVKGDVDGS IEALSDSLIK LSTEEIQVNV IHKAVGGIAE SDIMLAAASN
AIVIGFQVRP SLAARKVAEK EQIDIRLYSI IYDAIEEIKS AMEGMLSPEI KEQITSTVEV
RETFKITKVG TVAGCMVKEG KIRRNSKIRI IRDGIVIYTG ELGSLKRFKE DAKEVASGFE
CGLNVHNYND IKVGDLIESY EEVEVSRKL
//
