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Database: UniProt
Entry: A0A0S8ABJ3_9BACT
LinkDB: A0A0S8ABJ3_9BACT
Original site: A0A0S8ABJ3_9BACT 
ID   A0A0S8ABJ3_9BACT        Unreviewed;       699 AA.
AC   A0A0S8ABJ3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Tr-type G domain-containing protein {ECO:0000259|PROSITE:PS51722};
GN   ORFNames=AMS18_01815 {ECO:0000313|EMBL:KPJ95993.1};
OS   Gemmatimonas sp. SG8_17.
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatimonas.
OX   NCBI_TaxID=1703355 {ECO:0000313|EMBL:KPJ95993.1, ECO:0000313|Proteomes:UP000051607};
RN   [1] {ECO:0000313|EMBL:KPJ95993.1, ECO:0000313|Proteomes:UP000051607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_17 {ECO:0000313|EMBL:KPJ95993.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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}.
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:KPJ95993.1}.
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DR   EMBL; LJNM01000017; KPJ95993.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8ABJ3; -.
DR   PATRIC; fig|1703355.3.peg.2845; -.
DR   Proteomes; UP000051607; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro.
DR   CDD; cd04170; EF-G_bact; 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   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; 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   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; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          7..282
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   699 AA;  76820 MW;  033FBD030AB060DC CRC64;
     MRVYAGDAIR NVAVVGHGAS GKTTLVDALA FVAGSSKRHG SVPDGTALTD YTPDEIERKY
     SISLALAYAE WMDTKINLID TPGYLDFTGD AMAGIYAADA VLVVVGATSG VEVGTEKVWE
     YAVQREVPRL FMVTMLDKEH ADFERVYRDI KEHLTTGVVP VEIPLGEGPE FHGIVNLFSK
     KCHMYKPGTK TGEYEEVDVP EQHRERLEQY SQDLIETIAT TDDAMLERYL SGEEITRDEA
     IAALKAGMTK GELYPLLCGS AQLTYGMQAL LTKLVEVVPA PTECPAVVAQ KWGSAEEIGL
     TAQDDGPFVG QVFKTVSEPH VGDVSLFRIY SGRIGNGAEV YNAPRGVQEK LNHLSVALGK
     ERSEVLELHA GDIGVVAKLK DTHTNDTLSM QSTQVVIPKI PFPEPLIVMA IAVTTRGEED
     KLSTGLQKLH DEDPTFHHQF NAELRQTLIS GRGERHLEII VNRLERKFGV HSQLLKPKVA
     YRETFRGKGE GQGKHKKQSG GRGQYGDCWV RIAPRPGGSG YEFVNSVVGG AIPSKYIPAV
     DRGIQEAAAR GVLAGAPVVD FMAECYDGSY HNVDSSEQSF KMAGIMAFRN VAAKCKPVIL
     EPIFEIEVWT PDDNLGDVMG DLSSRRGQIL GTEQDRRLIK VKALVPEAEM YRYSTQLHSL
     TRGRGTFTWK FSSYQDVPSD VAQKIVEERQ KEDEEAAKG
//
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