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
//