ID   EFG_MYCTU               Reviewed;         701 AA.
AC   P9WNM7; L0T7E8; O53790; P0A556;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Elongation factor G;
DE            Short=EF-G;
GN   Name=fusA; OrderedLocusNames=Rv0684; ORFNames=MTCY210.01, MTV040.12;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   PUPYLATION AT LYS-307, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA   Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA   Gygi S.P., Darwin K.H.;
RT   "Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT   tuberculosis.";
RL   PLoS ONE 5:E8589-E8589(2010).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; AL123456; CCP43427.1; -; Genomic_DNA.
DR   PIR; E70827; E70827.
DR   RefSeq; WP_003898554.1; NZ_NVQJ01000007.1.
DR   RefSeq; YP_177746.1; NC_000962.3.
DR   PDB; 7CDW; X-ray; 3.00 A; A/B=1-701.
DR   PDBsum; 7CDW; -.
DR   AlphaFoldDB; P9WNM7; -.
DR   SMR; P9WNM7; -.
DR   STRING; 83332.Rv0684; -.
DR   PaxDb; P9WNM7; -.
DR   GeneID; 45424646; -.
DR   GeneID; 888240; -.
DR   KEGG; mtu:Rv0684; -.
DR   TubercuList; Rv0684; -.
DR   eggNOG; COG0480; Bacteria.
DR   OMA; AATTCHW; -.
DR   PhylomeDB; P9WNM7; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Elongation factor; GTP-binding; Isopeptide bond;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..701
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091165"
FT   DOMAIN          11..287
FT                   /note="tr-type G"
FT   BINDING         20..27
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         84..88
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         138..141
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        307
FT                   /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT                   with Q-Cter in protein Pup)"
FT                   /evidence="ECO:0000269|PubMed:20066036"
FT   HELIX           10..12
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          13..20
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   HELIX           26..39
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   TURN            43..45
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          68..75
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          78..83
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   HELIX           93..101
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          103..110
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   TURN            111..113
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   HELIX           117..128
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          133..138
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   HELIX           147..158
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          162..171
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   HELIX           172..174
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          177..180
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   TURN            181..184
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          185..188
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          200..202
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   HELIX           206..208
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   HELIX           209..226
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   HELIX           228..235
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   HELIX           242..254
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          259..263
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   TURN            266..269
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   HELIX           272..282
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   TURN            286..288
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          292..295
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          302..306
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          315..324
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   TURN            325..327
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          328..341
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          345..348
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   TURN            349..351
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          354..356
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          360..375
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          379..382
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          393..395
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          397..399
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          402..404
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          412..421
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   HELIX           422..438
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          443..447
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   TURN            448..451
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          452..459
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   HELIX           460..472
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          478..480
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          488..491
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          495..504
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          507..509
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          511..521
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          530..534
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   HELIX           543..545
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   HELIX           546..557
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          561..564
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          569..578
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   TURN            581..583
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   HELIX           586..602
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          606..619
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   HELIX           621..633
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          637..644
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          647..655
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   HELIX           656..658
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   HELIX           662..669
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   TURN            670..672
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   STRAND          675..685
FT                   /evidence="ECO:0007829|PDB:7CDW"
FT   HELIX           688..700
FT                   /evidence="ECO:0007829|PDB:7CDW"
SQ   SEQUENCE   701 AA;  77203 MW;  0C6DD4C128E31EA1 CRC64;
     MAQKDVLTDL SRVRNFGIMA HIDAGKTTTT ERILYYTGIN YKIGEVHDGA ATMDWMEQEQ
     ERGITITSAA TTTFWKDNQL NIIDTPGHVD FTVEVERNLR VLDGAVAVFD GKEGVEPQSE
     QVWRQADKYD VPRICFVNKM DKIGADFYFS VRTMGERLGA NAVPIQLPVG AEADFEGVVD
     LVEMNAKVWR GETKLGETYD TVEIPADLAE QAEEYRTKLL EVVAESDEHL LEKYLGGEEL
     TVDEIKGAIR KLTIASEIYP VLCGSAFKNK GVQPMLDAVV DYLPSPLDVP PAIGHAPAKE
     DEEVVRKATT DEPFAALAFK IATHPFFGKL TYIRVYSGTV ESGSQVINAT KGKKERLGKL
     FQMHSNKENP VDRASAGHIY AVIGLKDTTT GDTLSDPNQQ IVLESMTFPD PVIEVAIEPK
     TKSDQEKLSL SIQKLAEEDP TFKVHLDSET GQTVIGGMGE LHLDILVDRM RREFKVEANV
     GKPQVAYKET IKRLVQNVEY THKKQTGGSG QFAKVIINLE PFTGEEGATY EFESKVTGGR
     IPREYIPSVD AGAQDAMQYG VLAGYPLVNL KVTLLDGAYH EVDSSEMAFK IAGSQVLKKA
     AALAQPVILE PIMAVEVTTP EDYMGDVIGD LNSRRGQIQA MEERAGARVV RAHVPLSEMF
     GYVGDLRSKT QGRANYSMVF DSYSEVPANV SKEIIAKATG E