EFG2_PSEAE
ID EFG2_PSEAE Reviewed; 702 AA.
AC Q9I244;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Elongation factor G 2 {ECO:0000255|HAMAP-Rule:MF_00054};
DE Short=EF-G 2 {ECO:0000255|HAMAP-Rule:MF_00054};
GN Name=fusB; Synonyms=fusA2; OrderedLocusNames=PA2071;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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:0000255|HAMAP-
CC Rule:MF_00054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00054}.
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DR EMBL; AE004091; AAG05459.1; -; Genomic_DNA.
DR PIR; G83386; G83386.
DR RefSeq; NP_250761.1; NC_002516.2.
DR RefSeq; WP_003114863.1; NZ_QZGE01000022.1.
DR AlphaFoldDB; Q9I244; -.
DR SMR; Q9I244; -.
DR STRING; 287.DR97_5775; -.
DR PaxDb; Q9I244; -.
DR PRIDE; Q9I244; -.
DR EnsemblBacteria; AAG05459; AAG05459; PA2071.
DR GeneID; 879566; -.
DR KEGG; pae:PA2071; -.
DR PATRIC; fig|208964.12.peg.2160; -.
DR PseudoCAP; PA2071; -.
DR HOGENOM; CLU_002794_4_1_6; -.
DR InParanoid; Q9I244; -.
DR OMA; NHKMGEV; -.
DR PhylomeDB; Q9I244; -.
DR BioCyc; PAER208964:G1FZ6-2109-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd03713; EFG_mtEFG_C; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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; 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_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_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 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; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00484; EF-G; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..702
FT /note="Elongation factor G 2"
FT /id="PRO_0000091185"
FT DOMAIN 8..291
FT /note="tr-type G"
FT REGION 293..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 89..93
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 143..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ SEQUENCE 702 AA; 77574 MW; 4E02BDB47CC97859 CRC64;
MARTTPIELY RNIGIVAHVD AGKTTTTERI LFYTGVNHKM GEVHDGAATM DWMVQEQERG
ITITSAATTA FWQGSTKQFP HRYRFNIIDT PGHVDFTIEV ERSLRVLDGA VVVFSGADGV
EPQSETVWRQ ANKYHVPRLA YVNKMDRQGA DFLRVVAQIK QRLGHVPVPI QLAIGSEENF
SGQIDLVKMK AIYWNDADQG TSYREEEIPA ELRALAEEWR AHMVEAAAEA NDELMNKYLE
GEELSIEEIK AGLRQRTLAN QIVPAVLGSS FKNKGVPLVL DAVIDYLPAP SEIPAIRGTD
PDDEEKHDER HADDDEPFSA LAFKIATDPF VGTLTFARVY SGVLTSGDAV LNSVKGKKER
VGRMVQMHAN QRDEIKEVRA GDIAALIGMK DVTTGDTLCA IDKPIILERM DFPDPVISVA
VEPKTKADQE KMGIALSKLA QEDPSFRVKT DEETAQTIIS GMGELHLDII VDRMRREFGV
EANIGKPQVA YRETIRNTCE IEGKFVRQSG GRGQFGHCWI RFAPADEGQE GLEFHNEVVG
GVIPREFIPA IQKGIEDQMQ NGVLAGYPLI GLKATVYDGS YHDVDSSEMA FKIAASMATK
QLSQKGGAVL LEPVMKVEVV TPEDYMGDVM GDLNRRRGLI QGMEDTPAGK VIRAEVPLGE
MFGYATDVRS MSQGRASYSM EFVRYAEVPA SVAEGIVARQ GR
