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Database: UniProt
Entry: A0A0F7K2S3_9GAMM
LinkDB: A0A0F7K2S3_9GAMM
Original site: A0A0F7K2S3_9GAMM 
ID   A0A0F7K2S3_9GAMM        Unreviewed;       682 AA.
AC   A0A0F7K2S3;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Elongation factor G {ECO:0000256|ARBA:ARBA00017872};
GN   ORFNames=AAY24_13610 {ECO:0000313|EMBL:AKH21228.1};
OS   Sedimenticola thiotaurini.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Sedimenticola.
OX   NCBI_TaxID=1543721 {ECO:0000313|EMBL:AKH21228.1, ECO:0000313|Proteomes:UP000034410};
RN   [1] {ECO:0000313|EMBL:AKH21228.1, ECO:0000313|Proteomes:UP000034410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SIP-G1 {ECO:0000313|EMBL:AKH21228.1,
RC   ECO:0000313|Proteomes:UP000034410};
RX   PubMed=26089430;
RA   Flood B.E., Jones D.S., Bailey J.V.;
RT   "Complete Genome Sequence of Sedimenticola thiotaurini Strain SIP-G1, a
RT   Polyphosphate- and Polyhydroxyalkanoate-Accumulating Sulfur-Oxidizing
RT   Gammaproteobacterium Isolated from Salt Marsh Sediments.";
RL   Genome Announc. 3:e00671-15(2015).
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DR   EMBL; CP011412; AKH21228.1; -; Genomic_DNA.
DR   RefSeq; WP_046860157.1; NZ_CP011412.1.
DR   AlphaFoldDB; A0A0F7K2S3; -.
DR   KEGG; seds:AAY24_13610; -.
DR   PATRIC; fig|1543721.4.peg.2819; -.
DR   OrthoDB; 9804431at2; -.
DR   Proteomes; UP000034410; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd16262; EFG_III; 1.
DR   CDD; cd03713; EFG_mtEFG_C; 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; IPR035649; EFG_V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR004161; EFTu-like_2.
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; IPR005517; Transl_elong_EFG/EF2_IV.
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; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022768};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034410}.
FT   DOMAIN          8..279
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   682 AA;  74821 MW;  81F589090B166129 CRC64;
     MKNSPSIDKV RNIGIAAHID AGKTTLTERI LFYTGALYKI GEVHDGAAHM DYMAEEQSHG
     ITITSALTKA TWNDCLIQII DTPGHVDFTI EVERSMRVLD GCVIVLDGVR GVEPQTETVW
     RQRSKFNLPC LFFVNKIDRP GASFEHVLTT ISKRLGARPL PVTVPLPEQN AVIHLIEGTL
     IRFSGQHGDQ LETSPCDGAL WASVADHRET LLMGIAETDD LFADQVLAGE EPAPEQIWAA
     LRSATLRGEV CPCFGGSALR DLGIQPLIDG MTRLLPAPLE RPAATAWLPD GSTTTIEMED
     DQPLVALAFK VQMWDGRRHV FARIYRGTLK PGDQVRFSRA DGSMVQEHVA RIFDVDAARK
     TRIDIAHAGD IVLLAGLRHA ATGDTLCHPD HPLLLERIDT REPVLSLAVE PASSSQEEKF
     LEVMGKLQEE DPTLQFGEDP DTGQNLLRGM GELHLQIIIE RLQREYNLEV RTGKPAVALR
     ETITRQQELT QLFQPPADPA RKDSLKAQVT VLVKPLPRGT GLVRHCQPTV LPEGSQLTAQ
     QQEALEQGIQ FALGGGPLEG APLQDLEVSI TQVELFGAQS TPEALTSATA RALRKALESA
     GPALLQPIMK VEVMVPEENL GTVLGDLQSR HALIQDTDRT IDQATIHCEA PLASLLGYTT
     ELRSMTQGRG QFSTLFERFD ID
//
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