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Database: UniProt
Entry: A0A088SZ13_9BACT
LinkDB: A0A088SZ13_9BACT
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ID   A0A088SZ13_9BACT        Unreviewed;       689 AA.
AC   A0A088SZ13;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Elongation factor G {ECO:0000256|HAMAP-Rule:MF_00054};
DE            Short=EF-G {ECO:0000256|HAMAP-Rule:MF_00054};
GN   Name=fusA_1 {ECO:0000313|EMBL:AIO18035.1};
GN   Synonyms=fusA {ECO:0000256|HAMAP-Rule:MF_00054};
GN   ORFNames=KQ51_00131 {ECO:0000313|EMBL:AIO18035.1};
OS   Candidatus Izimaplasma bacterium HR1.
OC   Bacteria; Mycoplasmatota; Candidatus Izimaplasma.
OX   NCBI_TaxID=1541959 {ECO:0000313|EMBL:AIO18035.1, ECO:0000313|Proteomes:UP000029408};
RN   [1] {ECO:0000313|Proteomes:UP000029408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HR1 {ECO:0000313|Proteomes:UP000029408};
RA   Skennerton C.T., Haroon M.F., Tyson G.W., Orphan V.J.;
RT   "Phylogenomic Analysis of Candidatus Izimaplasma species: Representatives
RT   from a Novel Mollicute Clade found in Ocean Sediments.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AIO18035.1, ECO:0000313|Proteomes:UP000029408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HR1 {ECO:0000313|EMBL:AIO18035.1,
RC   ECO:0000313|Proteomes:UP000029408};
RX   PubMed=27058507; DOI=10.1038/ismej.2016.55;
RA   Skennerton C.T., Haroon M.F., Briegel A., Shi J., Jensen G.J., Tyson G.W.,
RA   Orphan V.J.;
RT   "Phylogenomic analysis of Candidatus 'Izimaplasma' species: free-living
RT   representatives from a Tenericutes clade found in methane seeps.";
RL   ISME J. 10:2679-2692(2016).
CC   -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC       during translation elongation. During this step, the ribosome changes
CC       from the pre-translocational (PRE) to the post-translocational (POST)
CC       state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC       deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC       coordinated movement of the two tRNA molecules, the mRNA and
CC       conformational changes in the ribosome. {ECO:0000256|HAMAP-
CC       Rule:MF_00054}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00054}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC       subfamily. {ECO:0000256|ARBA:ARBA00005870, ECO:0000256|HAMAP-
CC       Rule:MF_00054}.
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DR   EMBL; CP009415; AIO18035.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A088SZ13; -.
DR   STRING; 1541959.KQ51_00131; -.
DR   KEGG; mbj:KQ51_00131; -.
DR   PATRIC; fig|1541959.3.peg.125; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_1_14; -.
DR   OrthoDB; 9804431at2; -.
DR   Proteomes; UP000029408; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01886; EF-G; 1.
DR   CDD; cd16262; EFG_III; 1.
DR   CDD; cd01434; EFG_mtEFG1_IV; 1.
DR   CDD; cd03713; EFG_mtEFG_C; 1.
DR   CDD; cd04088; EFG_mtEFG_II; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.240; -; 1.
DR   Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR   InterPro; IPR041095; EFG_II.
DR   InterPro; IPR009022; EFG_III.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR047872; EFG_IV.
DR   InterPro; IPR035649; EFG_V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR004540; Transl_elong_EFG/EF2.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   NCBIfam; TIGR00484; EF-G; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43261:SF1; RIBOSOME-RELEASING FACTOR 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43261; TRANSLATION ELONGATION FACTOR G-RELATED; 1.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF14492; EFG_III; 1.
DR   Pfam; PF03764; EFG_IV; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 1.
DR   SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00054};
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW   Rule:MF_00054};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00054};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00054};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00054}; Reference proteome {ECO:0000313|Proteomes:UP000029408}.
FT   DOMAIN          8..282
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         17..24
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT   BINDING         81..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT   BINDING         135..138
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   689 AA;  76039 MW;  A77B6E71D43A06C9 CRC64;
     MAREYSLKMT RNIGIMAHID AGKTTCTERI LYHTGKIHKI GETHDGASQM DWMAQEQERG
     ITITSAATTA HWKEHRVNII DTPGHVDFTV EVSRSLRVLD GSVALLDAQA GVEPQTETVW
     RQANDYKVPR IVFANKMDKI GADFEFSVKT LEDRLGANAA AIQWPIGAEN DFDGIIDLVE
     MKAWHFDGGA DEMPTEMEIP EYLQEKVEAK RMELIETVAD FDEELMMMYL EGEEIDGKTL
     KAAVRNATLA VEFFPVLCGS AFKNKGVKLL LDAVIAYLPS PLDVAAVVGT NKKGDDVVLE
     ASDEGQFSAL AFKVMTDPFV GKLTFFRVYS GKLAKGSYIR NATKDKKERV GRILQMHANS
     REEVDMVFSG DIAAAVGLKN TTTGDTLCAD KSYIILEKMV FPEPVISVAI EPNSRADQDK
     MGIALSKLAE EDPTFRTYTD QETGQTIISG MGELHLDIIV DRMKREFKVE ANVGAPQVSY
     RETITTSAEI EGKFVRQSGG RGQYGHVWIR FEPNPEKGFE FVDKIVGGVV PREYIPVVGK
     GLNEQLASGI LAGYPLIDLK ATLYDGSYHD VDSNEMAFKV AAGMALKKAK DACNAILLEP
     IMTVDVIIPD EYLGNVIGDI TSRRGRIEGQ SQRGNAQQVT AKVPLAEMFG YATSLRSNTQ
     GRGNYVMQPS HYEACPRSIA DEVIKKRNG
//
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