ID A0A017RUT5_9CLOT Unreviewed; 705 AA.
AC A0A017RUT5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=Q428_09110 {ECO:0000313|EMBL:EYE88179.1};
OS Fervidicella metallireducens AeB.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Fervidicella.
OX NCBI_TaxID=1403537 {ECO:0000313|EMBL:EYE88179.1, ECO:0000313|Proteomes:UP000019681};
RN [1] {ECO:0000313|EMBL:EYE88179.1, ECO:0000313|Proteomes:UP000019681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AeB {ECO:0000313|EMBL:EYE88179.1,
RC ECO:0000313|Proteomes:UP000019681};
RX PubMed=24786951;
RA Patel B.K.;
RT "Draft Genome Sequence of Fervidicella metallireducens Strain AeBT, an
RT Iron-Reducing Thermoanaerobe from the Great Artesian Basin.";
RL Genome Announc. 2:e00345-14(2014).
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|ARBA:ARBA00025162, ECO:0000256|HAMAP-
CC Rule:MF_00100, 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: 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:EYE88179.1}.
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DR EMBL; AZQP01000026; EYE88179.1; -; Genomic_DNA.
DR RefSeq; WP_035380102.1; NZ_AZQP01000026.1.
DR AlphaFoldDB; A0A017RUT5; -.
DR STRING; 1403537.Q428_09110; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000019681; 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; 2.
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:UP000019681}.
FT DOMAIN 206..373
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 91..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..357
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 91..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 215..222
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 261..265
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 315..318
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 705 AA; 77724 MW; 8FC169AE1A208719 CRC64;
MSKIRIYELA KQTNMSSKEL IDLLNKEFGL EVKNHMSVIE GEEANIILEY FGELHQNDLT
EGKMEEINSP ISEIDEYELL QETEFYDEKK GRKKVKSDKS KNNGSSRLNK NEMNKDTAIE
QEIGMVTIPE SIKVGEFARL INKPSSEIIK KLLFMGVMAT INHEITFETA EKIAEEYNII
VDKEIKKEKE EILINDFEDD EESLQVRPPV VTVMGHVDHG KTSLLDAIRH SKVTETEAGG
ITQHIGAYTV DINGSKVTFL DTPGHEAFTA MRARGAQATD IAILVVAADD GVMPQTVEAI
NHAKAANVPI IVAINKMDKP NANPDRVKQE LTEYGLIAED WGGDTVCVPV SAKSKIGIDN
LLEMILLVAE IQQLTANPNR PAKGIIIEAK LDKGRGPVAT VLVQKGTLRI GDAIVAGVAY
GKVRAMVDDK GRKVKEAGPS IPVEVLGLSE VPNAGDILYC VSDDKTARQI GEIRKNKERQ
EHYANTAKVS LEDLFSQIQS GKVKDLNIIV KADVQGSVEA VKQSLEKISN EEVRVNVIHG
AVGAITETDV ALAAASNAII IGFNVRPDNM ARQAADRENV DVKTYRIIYE AIDDITAAMK
GMLDPEYKEV VTARLSVRTT FKVSSVGTIA GCYVEDGKIN RNNDIRVIRN GVVVFEGKIS
SLKRFKDDVK EVASGFECGL TIERFNDIKE GDTIEAYTME EVERK
//
