EFG_STAAU
ID EFG_STAAU Reviewed; 693 AA.
AC P68790; P81683; Q9X7M3;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Elongation factor G;
DE Short=EF-G;
DE AltName: Full=85 kDa vitronectin-binding protein;
GN Name=fusA; Synonyms=fus;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11309125; DOI=10.1046/j.1365-2958.2001.02389.x;
RA Nagaev I., Bjorkman J., Andersson J., Hughes D.;
RT "Biological cost and compensatory evolution in fusidic acid-resistant
RT Staphylococcus aureus.";
RL Mol. Microbiol. 40:433-439(2001).
RN [2]
RP PROTEIN SEQUENCE OF 2-26.
RC STRAIN=ATCC 12598 / Cowan 1 / DSM 20372 / NCIMB 11787 / NCTC 8530;
RA Hussain M.S., Herrmann M., Chhatwal G.S., Peters G.;
RT "A 85 kDa vitronectin binding protein of Staphylococcus aureus Cowan 1.";
RL Submitted (FEB-1999) to UniProtKB.
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.
CC -!- SUBUNIT: Has vitronectin-binding activity.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ237696; CAB40191.1; -; Genomic_DNA.
DR RefSeq; WP_000090315.1; NZ_WYDB01000005.1.
DR PDB; 2XEX; X-ray; 1.90 A; A/B=1-693.
DR PDB; 3ZZ0; X-ray; 2.80 A; A/B=1-693.
DR PDB; 3ZZT; X-ray; 2.95 A; A/B=1-693.
DR PDB; 3ZZU; X-ray; 2.98 A; A/B=1-693.
DR PDBsum; 2XEX; -.
DR PDBsum; 3ZZ0; -.
DR PDBsum; 3ZZT; -.
DR PDBsum; 3ZZU; -.
DR AlphaFoldDB; P68790; -.
DR SMR; P68790; -.
DR ChEMBL; CHEMBL4665583; -.
DR OMA; AATTCHW; -.
DR EvolutionaryTrace; P68790; -.
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; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Elongation factor;
KW GTP-binding; Nucleotide-binding; Protein biosynthesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..693
FT /note="Elongation factor G"
FT /id="PRO_0000091219"
FT DOMAIN 8..282
FT /note="tr-type G"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 135..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 4
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 19
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="T -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:3ZZ0"
FT STRAND 10..16
FT /evidence="ECO:0007829|PDB:2XEX"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:2XEX"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:2XEX"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:2XEX"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:2XEX"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:2XEX"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:2XEX"
FT HELIX 114..125
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:2XEX"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:2XEX"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:2XEX"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:2XEX"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:2XEX"
FT HELIX 204..219
FT /evidence="ECO:0007829|PDB:2XEX"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:2XEX"
FT HELIX 237..249
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:2XEX"
FT TURN 261..264
FT /evidence="ECO:0007829|PDB:2XEX"
FT HELIX 267..277
FT /evidence="ECO:0007829|PDB:2XEX"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 294..301
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:3ZZ0"
FT STRAND 310..319
FT /evidence="ECO:0007829|PDB:2XEX"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 323..336
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:2XEX"
FT TURN 344..347
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 348..352
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 374..379
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 407..416
FT /evidence="ECO:0007829|PDB:2XEX"
FT HELIX 417..433
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 448..454
FT /evidence="ECO:0007829|PDB:2XEX"
FT HELIX 455..468
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 483..488
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 490..498
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 505..515
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 523..526
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 530..533
FT /evidence="ECO:0007829|PDB:3ZZ0"
FT HELIX 535..537
FT /evidence="ECO:0007829|PDB:2XEX"
FT HELIX 538..550
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 553..556
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 561..570
FT /evidence="ECO:0007829|PDB:2XEX"
FT TURN 573..575
FT /evidence="ECO:0007829|PDB:2XEX"
FT HELIX 578..593
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 598..612
FT /evidence="ECO:0007829|PDB:2XEX"
FT HELIX 613..615
FT /evidence="ECO:0007829|PDB:2XEX"
FT HELIX 616..625
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 629..636
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 639..647
FT /evidence="ECO:0007829|PDB:2XEX"
FT HELIX 648..650
FT /evidence="ECO:0007829|PDB:2XEX"
FT HELIX 654..661
FT /evidence="ECO:0007829|PDB:2XEX"
FT TURN 662..664
FT /evidence="ECO:0007829|PDB:2XEX"
FT STRAND 667..677
FT /evidence="ECO:0007829|PDB:2XEX"
FT HELIX 680..690
FT /evidence="ECO:0007829|PDB:2XEX"
SQ SEQUENCE 693 AA; 76612 MW; BAE273E3A33EEED9 CRC64;
MAREFSLEKT RNIGIMAHID AGKTTTTERI LYYTGRIHKI GETHEGASQM DWMEQEQDRG
ITITSAATTA AWEGHRVNII DTPGHVDFTV EVERSLRVLD GAVTVLDAQS GVEPQTETVW
RQATTYGVPR IVFVNKMDKL GANFEYSVST LHDRLQANAA PIQLPIGAED EFEAIIDLVE
MKCFKYTNDL GTEIEEIEIP EDHLDRAEEA RASLIEAVAE TSDELMEKYL GDEEISVSEL
KEAIRQATTN VEFYPVLCGT AFKNKGVQLM LDAVIDYLPS PLDVKPIIGH RASNPEEEVI
AKADDSAEFA ALAFKVMTDP YVGKLTFFRV YSGTMTSGSY VKNSTKGKRE RVGRLLQMHA
NSRQEIDTVY SGDIAAAVGL KDTGTGDTLC GEKNDIILES MEFPEPVIHL SVEPKSKADQ
DKMTQALVKL QEEDPTFHAH TDEETGQVII GGMGELHLDI LVDRMKKEFN VECNVGAPMV
SYRETFKSSA QVQGKFSRQS GGRGQYGDVH IEFTPNETGA GFEFENAIVG GVVPREYIPS
VEAGLKDAME NGVLAGYPLI DVKAKLYDGS YHDVDSSEMA FKIAASLALK EAAKKCDPVI
LEPMMKVTIE MPEEYMGDIM GDVTSRRGRV DGMEPRGNAQ VVNAYVPLSE MFGYATSLRS
NTQGRGTYTM YFDHYAEVPK SIAEDIIKKN KGE
