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Database: UniProt
Entry: A0A1C4M5N3_9ACTN
LinkDB: A0A1C4M5N3_9ACTN
Original site: A0A1C4M5N3_9ACTN 
ID   A0A1C4M5N3_9ACTN        Unreviewed;       709 AA.
AC   A0A1C4M5N3;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
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 {ECO:0000256|HAMAP-Rule:MF_00054};
GN   ORFNames=GA0115234_1049118 {ECO:0000313|EMBL:SCD81235.1};
OS   Streptomyces sp. DvalAA-43.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1839762 {ECO:0000313|EMBL:SCD81235.1, ECO:0000313|Proteomes:UP000199186};
RN   [1] {ECO:0000313|EMBL:SCD81235.1, ECO:0000313|Proteomes:UP000199186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DvalAA-43 {ECO:0000313|EMBL:SCD81235.1,
RC   ECO:0000313|Proteomes:UP000199186};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00024731,
CC       ECO:0000256|HAMAP-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; FMBW01000037; SCD81235.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4M5N3; -.
DR   OrthoDB; 9801472at2; -.
DR   Proteomes; UP000199186; Unassembled WGS sequence.
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}.
FT   DOMAIN          9..296
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          300..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         18..25
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT   BINDING         86..90
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT   BINDING         140..143
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   709 AA;  77677 MW;  9BEFD1A22B677272 CRC64;
     MATTSLDLAK VRNIGIMAHI DAGKTTTTER ILFYTGVSYK IGEVHDGAAT MDWMEQEQER
     GITITSAATT CHWPLNDVDH TINIIDTPGH VDFTVEVERS LRVLDGAVTV FDGVAGVEPQ
     SETVWRQADR YGVPRICFVN KLDRTGADFL RCVQMIVDRL GATPIVMQLP IGAEADFTGV
     VDLVSMRAFV YPEEAAKGEM YNIVEIPDNL KEAAEEWRGK LLEAVAENDD AMMELYLEGN
     EPTQEQLHEA IRRITLASKG GADSVTVTPV FCGTAFKNKG VQPLLDAVVR YLPSPLDVEA
     IEGHDPKDPE KVIERKPSDD EPFSGLAFKI ASDPHLGKLT FVRIYSGRLE AGTAVLNSVK
     GKKERIGKIY RMHANKREEI ASVGAGDIIA VMGLKQTTTG ETLCDDKNPV ILESMDFPAP
     VIQVAIEPKS KGDQEKLGVA IQRLSEEDPS FQVHSDEETG QTIIGGMGEL HLEVLVDRMK
     REFRVEANVG KPQVAYRETI RKAVERIDYT HKKQTGGTGQ FAKVQIALEP IEGGDASYEF
     VNKVTGGRIP REYIPSVDAG AQEAMQFGIL AGYEMVGVRV TLLDGGYHEV DSSELAFKIA
     GSQAFKEGAR KASPVLLEPM MAVEVTTPED YMGDVIGDLN SRRGQIQAME ERSGARVVKG
     LVPLSEMFGY VGDLRSKTSG RASYSMQFDS YAEVPRNVAE EIIAKAKGE
//
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