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Database: UniProt
Entry: A6TWL9_ALKMQ
LinkDB: A6TWL9_ALKMQ
Original site: A6TWL9_ALKMQ 
ID   A6TWL9_ALKMQ            Unreviewed;       689 AA.
AC   A6TWL9;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   24-JAN-2024, entry version 101.
DE   RecName: Full=Elongation factor G {ECO:0000256|ARBA:ARBA00017872};
GN   OrderedLocusNames=Amet_4515 {ECO:0000313|EMBL:ABR50587.1};
OS   Alkaliphilus metalliredigens (strain QYMF).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=293826 {ECO:0000313|EMBL:ABR50587.1, ECO:0000313|Proteomes:UP000001572};
RN   [1] {ECO:0000313|Proteomes:UP000001572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QYMF {ECO:0000313|Proteomes:UP000001572};
RX   PubMed=27811105; DOI=10.1128/genomeA.01226-16;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA   Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA   Richardson P., Fields M.W.;
RT   "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT   alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT   leachate ponds.";
RL   Genome Announc. 4:0-0(2016).
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}.
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DR   EMBL; CP000724; ABR50587.1; -; Genomic_DNA.
DR   RefSeq; WP_012065478.1; NC_009633.1.
DR   AlphaFoldDB; A6TWL9; -.
DR   STRING; 293826.Amet_4515; -.
DR   KEGG; amt:Amet_4515; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_1_9; -.
DR   OMA; KPKIAYR; -.
DR   OrthoDB; 9804431at2; -.
DR   Proteomes; UP000001572; Chromosome.
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:UniProtKB-KW.
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; 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; 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:SF6; ELONGATION FACTOR G-LIKE PROTEIN; 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   3: Inferred from homology;
KW   Elongation factor {ECO:0000313|EMBL:ABR50587.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:ABR50587.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001572}.
FT   DOMAIN          7..278
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          482..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..498
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   689 AA;  76330 MW;  74DC6CE218BDCE24 CRC64;
     MKSYQAANIR NIALLGHGGC GKTTLTEAIA YSAKLTNRMG RVEDGNTISD FDKEEIARGV
     SVGTTIVPIE WEGYKLNFLD TPGYFDFVGE VQSAMKVAGG AIIVLDATSG IEVGTEKSWE
     YISDSKKPTF IFVNKMDREN ANFDKVLTEL REKFGKKIAP FQIPLGEHEN FIGNVNIAKL
     VAREYNGKDC KERPIPEELK EQVDVFRELL LESVAESDEA LLEKYFAGET FTEEEIQKSL
     RKGVISGDII PVLCGSTLKN IGTHTLMDMI RDYSPSPLDM PAKQGKNPYN DEVVSRSLEV
     DQPFSAQVYK TVVDAYVGKI SLMKVISGKL TGDSEVLNAN KEEKEKIGPL FLLRGKNQID
     VTEAWAGDIV AVAKLQHTNT GDTLCNISDP ILYSNIEFDK PQLYLAIEPK AKGDEEKIGS
     GLQRLSEEDP SFTFERNAET RQTLICGHGE LHIKVIINKL KNKFGVDVRL IDPKVPYRET
     IKGRSDAQGK HKKQSGGHGQ YGDVRIRFEP AAGEFEFAEE VVGGSVPRSY IPAVEKGLRD
     CLVTGVLAGY PVTNIKATLY DGSYHDVDSS EMAFKIAASL AFKKGVEEAK PVLLEPVVKV
     NVFVPEEYMG DIMGDLNKRR GRILGMEPQP KGAQLVIAEV PQSEMFKYAT DLRSMTQARG
     SFQMEFSRYE EVPQSIAEKV VEAAQADRE
//
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