ID T0PKB8_9CLOT Unreviewed; 696 AA.
AC T0PKB8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=M918_05310 {ECO:0000313|EMBL:EQB88177.1};
OS Clostridium sp. BL8.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1354301 {ECO:0000313|EMBL:EQB88177.1, ECO:0000313|Proteomes:UP000015873};
RN [1] {ECO:0000313|EMBL:EQB88177.1, ECO:0000313|Proteomes:UP000015873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL8 {ECO:0000313|EMBL:EQB88177.1,
RC ECO:0000313|Proteomes:UP000015873};
RX PubMed=25076986; DOI=10.1186/1757-4749-6-30;
RA Marathe N.P., Shetty S.A., Lanjekar V.B., Rasane M.H., Ranade D.R.,
RA Shouche Y.S.;
RT "Genome sequencing of multidrug resistant novel Clostridium sp. BL8 reveals
RT its potential for pathogenicity.";
RL Gut Pathog. 6:30-30(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 -!- 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:EQB88177.1}.
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DR EMBL; AUPA01000164; EQB88177.1; -; Genomic_DNA.
DR RefSeq; WP_021283341.1; NZ_AUPA01000164.1.
DR AlphaFoldDB; T0PKB8; -.
DR STRING; 1354301.M918_05310; -.
DR PATRIC; fig|1354301.3.peg.2236; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000015873; 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 PRINTS; PR00315; ELONGATNFCT.
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.
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:UP000015873}.
FT DOMAIN 195..368
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 198..346
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 204..211
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 250..254
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 304..307
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 696 AA; 76681 MW; 516B74417AFA4654 CRC64;
MSKLRIYELA KELEISSKEL ITVLLEEFGI EAKNHMSVID EEDGDLIKEL YSEKKTSDED
KKEIVEEYEE LVNEDIKKQE RKNSKIKRGT NDKRDEDKKI ENSVDEVIEL EGTIVVKDLA
EKLKKPATEV IKALIFEGVM ANMNQEIDFN IAEKVIEKFG SLAVLKEAEA GKLAAEEVYA
ESIEDSEENE ENEEKRPPIV TVMGHVDHGK TSLLDAIKHS KVTSTEAGGI TQHIGAYTVD
VNGEKVTFLD TPGHEAFTAM RARGAQITDI VILVVAADDG IMPQTVEAIN HCKAAKVPMI
VAINKMDRPA ANPDKVKQEL TEHGLLSEDW GGDTICVPVS AHTREGLDTL LEMVILTSEM
LELNANPKRN AKGTVIEAKL DKGRGPLATL LVQNGTLSTG DSIIVGTTYG RIRAMLDDKG
KKIKAAGPSI PVEVLGLSEV PAAGDRFIVV KDEKTARNMA ESRKEKIRQE NFQSSNRVSM
ENLYSQIQEG KVKELSVIVK ADVQGSVEAI RQSIEKLSTD NVKVRVIHGG VGAITETDVS
LAYASNAIII GFNVRPDNNA IAVGERDNVE IKTYRIIYNA LDDIKAAMMG MLEPEYKEVV
LGRVEVRAVY KISNVGTIAG CYVLNGKITR NSSVRVLRQG IVIFESTLAS LKRFKDDVKE
AAAGFECGLS VEKFNDIKEG DIIEAYTMEE IKPKQI
//
