GenomeNet

Database: UniProt
Entry: H8GQC9_METAL
LinkDB: H8GQC9_METAL
Original site: H8GQC9_METAL 
ID   H8GQC9_METAL            Unreviewed;       694 AA.
AC   H8GQC9;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Elongation factor G {ECO:0000256|ARBA:ARBA00017872, 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=Metal_0755 {ECO:0000313|EMBL:EIC28588.1};
OS   Methylomicrobium album BG8.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylomicrobium.
OX   NCBI_TaxID=686340 {ECO:0000313|EMBL:EIC28588.1, ECO:0000313|Proteomes:UP000005090};
RN   [1] {ECO:0000313|EMBL:EIC28588.1, ECO:0000313|Proteomes:UP000005090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BG8 {ECO:0000313|EMBL:EIC28588.1,
RC   ECO:0000313|Proteomes:UP000005090};
RX   PubMed=23580712;
RA   Kits K.D., Kalyuzhnaya M.G., Klotz M.G., Jetten M.S., Op den Camp H.J.,
RA   Vuilleumier S., Bringel F., Dispirito A.A., Murrell J.C., Bruce D.,
RA   Cheng J.F., Copeland A., Goodwin L., Hauser L., Lajus A., Land M.L.,
RA   Lapidus A., Lucas S., Medigue C., Pitluck S., Woyke T., Zeytun A.,
RA   Stein L.Y.;
RT   "Genome Sequence of the Obligate Gammaproteobacterial Methanotroph
RT   Methylomicrobium album Strain BG8.";
RL   Genome Announc. 1:E0017013-E0017013(2013).
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|HAMAP-
CC       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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM001475; EIC28588.1; -; Genomic_DNA.
DR   RefSeq; WP_005369760.1; NZ_CM001475.1.
DR   AlphaFoldDB; H8GQC9; -.
DR   STRING; 686340.Metal_0755; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_1_6; -.
DR   Proteomes; UP000005090; Chromosome.
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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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:SF5; ELONGATION FACTOR G 1; 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}; Reference proteome {ECO:0000313|Proteomes:UP000005090}.
FT   DOMAIN          5..280
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         14..21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT   BINDING         78..82
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT   BINDING         132..135
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   694 AA;  76643 MW;  6D6F22D8DB577A86 CRC64;
     MTDLSLYRNI GIFAHVDAGK TTTTERILKL TGKIHKLGEV HEGESTMDFM AQEAERGITI
     QSAATTCFWK DHRFNIIDTP GHVDFTIEVY RSLKVLDGGI GVFCGSGGVE PQSETNWRYA
     NDSKVSRLIY VNKLDRIGAD FFRVVKQVED VLGAVPLVMT LPIGIEDQFS GVVDLLTRKA
     WIWDNSGDPM SYRIEDVPAD MADKVEEWRE KLIETAVEQD DDAMEKYLEG EEPDMETVKR
     CIRKGTINMA FFPTYCGSSF KNKGVQLVLD GVVDYLPNPT EVKPQPETDI EGNPTGEFAI
     VDPSRPLRAL VFKIMDDRFG ALNFIRIYSG RLKKGDTLLN TYTGKNERVG RMVEMHADTR
     TEIETAQAGD IVALIGLKNV QTGHTLCDPD KPATLEPMVF PDPVISVAVT PKDKGSNEKM
     GIALGKMVAE DPSFHVSTDE ESGETILKGM GELHLDIKVD ILKRTHGVEV TVGKPQVAYR
     ETITRRVEDE YTHKKQSGGS GQYAKISYAI EPGEPGSGFA FESAVTGGNV PREYWPAVEK
     GFKSMLDQGV LAGYPCLDFK VTLLDGGFHA VDSSSIAFEI AAKAAFRQSI PKAAPQLIEP
     IMKVDVFTPA DNVGDVIGDL NRRRGMIKSQ DPGVTGVRVK ADVPLSEMFG YIGDLRTMTS
     GRGQFSMEFS HYLPCPKNVA EEVIKEAIER KKAK
//
DBGET integrated database retrieval system