GSPE_VIBCH
ID GSPE_VIBCH Reviewed; 503 AA.
AC P37093; Q9JPZ4;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Type II secretion system ATPase E;
DE Short=T2SS protein E;
DE EC=7.4.2.8 {ECO:0000269|PubMed:15601709, ECO:0000269|PubMed:27168165};
DE AltName: Full=Cholera toxin secretion protein EpsE;
DE AltName: Full=General secretion pathway protein E;
DE AltName: Full=Type II traffic warden ATPase;
GN Name=epsE; OrderedLocusNames=VC_2732;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=El Tor TRH7000;
RX PubMed=8423007; DOI=10.1016/0378-1119(93)90543-c;
RA Sandkvist M., Morales V., Bagdasarian M.M.;
RT "A protein required for secretion of cholera toxin through the outer
RT membrane of Vibrio cholerae.";
RL Gene 123:81-86(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [3]
RP FUNCTION, ATPASE ACTIVITY, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-270,
RP SUBUNIT, AND COFACTOR.
RX PubMed=15601709; DOI=10.1128/jb.187.1.249-256.2005;
RA Camberg J.L., Sandkvist M.;
RT "Molecular analysis of the Vibrio cholerae type II secretion ATPase EpsE.";
RL J. Bacteriol. 187:249-256(2005).
RN [4]
RP SUBUNIT, AND MUTAGENESIS OF ARG-210; ARG-225; ARG-324 AND ARG-336.
RX PubMed=21209100; DOI=10.1074/jbc.m110.167031;
RA Patrick M., Korotkov K.V., Hol W.G., Sandkvist M.;
RT "Oligomerization of EpsE coordinates residues from multiple subunits to
RT facilitate ATPase activity.";
RL J. Biol. Chem. 286:10378-10386(2011).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND DISRUPTION PHENOTYPE.
RX PubMed=27168165; DOI=10.1002/mbo3.376;
RA Rule C.S., Patrick M., Camberg J.L., Maricic N., Hol W.G., Sandkvist M.;
RT "Zinc coordination is essential for the function and activity of the type
RT II secretion ATPase EpsE.";
RL MicrobiologyOpen 5:870-882(2016).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 91-498 IN COMPLEX WITH ATP ANALOG
RP AND ZINC.
RX PubMed=14556751; DOI=10.1016/j.jmb.2003.07.015;
RA Robien M.A., Krumm B.E., Sandkvist M., Hol W.G.;
RT "Crystal structure of the extracellular protein secretion NTPase EpsE of
RT Vibrio cholerae.";
RL J. Mol. Biol. 333:657-674(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-96, AND INTERACTION WITH EPSL.
RX PubMed=15843017; DOI=10.1016/j.jmb.2005.02.061;
RA Abendroth J., Murphy P., Sandkvist M., Bagdasarian M., Hol W.G.;
RT "The X-ray structure of the type II secretion system complex formed by the
RT N-terminal domain of EpsE and the cytoplasmic domain of EpsL of Vibrio
RT cholerae.";
RL J. Mol. Biol. 348:845-855(2005).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (4.20 ANGSTROMS) OF 100-503, AND SUBUNIT.
RX PubMed=23954505; DOI=10.1016/j.str.2013.06.027;
RA Lu C., Turley S., Marionni S.T., Park Y.J., Lee K.K., Patrick M., Shah R.,
RA Sandkvist M., Bush M.F., Hol W.G.;
RT "Hexamers of the type II secretion ATPase GspE from Vibrio cholerae with
RT increased ATPase activity.";
RL Structure 21:1707-1717(2013).
CC -!- FUNCTION: ATPase component of the type II secretion system required for
CC the energy-dependent secretion of extracellular factors such as
CC proteases and toxins from the periplasm. Acts as a molecular motor to
CC provide the energy that is required for assembly of the pseudopilus and
CC the extrusion of substrates generated in the cytoplasm.
CC {ECO:0000269|PubMed:15601709, ECO:0000269|PubMed:27168165}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC cellular proteinSide 2.; EC=7.4.2.8;
CC Evidence={ECO:0000269|PubMed:15601709, ECO:0000269|PubMed:27168165};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Removal of zinc reduces the enzymatic activity by about 2-fold.
CC {ECO:0000269|PubMed:15601709, ECO:0000269|PubMed:27168165};
CC -!- SUBUNIT: Forms homooligomers; most probably hexamers (PubMed:15601709,
CC PubMed:23954505) (Probable). Interacts with EpsL/GspL
CC (PubMed:15843017). {ECO:0000269|PubMed:15601709,
CC ECO:0000269|PubMed:15843017, ECO:0000269|PubMed:23954505,
CC ECO:0000305|PubMed:21209100}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:Q00512}. Note=Membrane association is not an
CC intrinsic property but requires the EpsL/GspL gene product.
CC {ECO:0000250|UniProtKB:Q00512}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants show complete loss of protease
CC secretion. {ECO:0000269|PubMed:27168165}.
CC -!- SIMILARITY: Belongs to the GSP E family. {ECO:0000305}.
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DR EMBL; M96172; AAA27518.1; -; Genomic_DNA.
DR EMBL; L33796; AAA58786.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF95872.1; -; Genomic_DNA.
DR PIR; JU0147; JU0147.
DR RefSeq; NP_232359.1; NC_002505.1.
DR RefSeq; WP_000138174.1; NZ_LT906614.1.
DR PDB; 1P9R; X-ray; 2.50 A; A=91-498.
DR PDB; 1P9W; X-ray; 2.70 A; A=91-498.
DR PDB; 2BH1; X-ray; 2.40 A; X/Y=1-96.
DR PDB; 4KSR; X-ray; 4.20 A; A/B/C=100-503.
DR PDB; 4KSS; X-ray; 7.58 A; A/B/C/D/E/F=100-503.
DR PDBsum; 1P9R; -.
DR PDBsum; 1P9W; -.
DR PDBsum; 2BH1; -.
DR PDBsum; 4KSR; -.
DR PDBsum; 4KSS; -.
DR AlphaFoldDB; P37093; -.
DR SMR; P37093; -.
DR STRING; 243277.VC_2732; -.
DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR DNASU; 2614895; -.
DR EnsemblBacteria; AAF95872; AAF95872; VC_2732.
DR GeneID; 57741324; -.
DR GeneID; 66938394; -.
DR KEGG; vch:VC_2732; -.
DR PATRIC; fig|243277.26.peg.2607; -.
DR eggNOG; COG2804; Bacteria.
DR HOGENOM; CLU_013446_10_3_6; -.
DR OMA; LIRKPHG; -.
DR BioCyc; VCHO:VC2732-MON; -.
DR BRENDA; 7.4.2.8; 6626.
DR EvolutionaryTrace; P37093; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015627; C:type II protein secretion system complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008564; F:protein-exporting ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IBA:GO_Central.
DR Gene3D; 3.30.300.160; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001482; T2SS/T4SS.
DR InterPro; IPR037257; T2SS_E_N_sf.
DR InterPro; IPR013369; T2SS_GspE.
DR Pfam; PF00437; T2SSE; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF160246; SSF160246; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02533; type_II_gspE; 1.
DR PROSITE; PS00662; T2SP_E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Metal-binding; Nucleotide-binding; Protein transport; Reference proteome;
KW Translocase; Transport; Zinc.
FT CHAIN 1..503
FT /note="Type II secretion system ATPase E"
FT /id="PRO_0000207290"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:1P9R, ECO:0007744|PDB:1P9W"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:1P9R, ECO:0007744|PDB:1P9W"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:1P9R, ECO:0007744|PDB:1P9W"
FT BINDING 433
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:1P9R, ECO:0007744|PDB:1P9W"
FT MUTAGEN 210
FT /note="R->A: More than 95% loss of protease secretion."
FT /evidence="ECO:0000269|PubMed:21209100"
FT MUTAGEN 225
FT /note="R->A: More than 95% loss of protease secretion."
FT /evidence="ECO:0000269|PubMed:21209100"
FT MUTAGEN 270
FT /note="K->A: About 3-fold loss of ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:15601709"
FT MUTAGEN 324
FT /note="R->A: More than 95% loss of protease secretion."
FT /evidence="ECO:0000269|PubMed:21209100"
FT MUTAGEN 336
FT /note="R->A: More than 95% loss of protease secretion."
FT /evidence="ECO:0000269|PubMed:21209100"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:2BH1"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:2BH1"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:2BH1"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:2BH1"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:2BH1"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:2BH1"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:2BH1"
FT HELIX 101..106
FT /evidence="ECO:0007829|PDB:1P9R"
FT HELIX 122..137
FT /evidence="ECO:0007829|PDB:1P9R"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:1P9R"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:1P9R"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:1P9R"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:1P9R"
FT HELIX 172..182
FT /evidence="ECO:0007829|PDB:1P9R"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:1P9R"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:1P9R"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:1P9R"
FT TURN 229..232
FT /evidence="ECO:0007829|PDB:1P9R"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:1P9R"
FT HELIX 243..253
FT /evidence="ECO:0007829|PDB:1P9R"
FT STRAND 255..263
FT /evidence="ECO:0007829|PDB:1P9R"
FT HELIX 270..281
FT /evidence="ECO:0007829|PDB:1P9R"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:1P9R"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:1P9R"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:1P9R"
FT HELIX 315..322
FT /evidence="ECO:0007829|PDB:1P9R"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:1P9R"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:1P9R"
FT HELIX 338..349
FT /evidence="ECO:0007829|PDB:1P9R"
FT STRAND 353..358
FT /evidence="ECO:0007829|PDB:1P9R"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:1P9R"
FT HELIX 364..373
FT /evidence="ECO:0007829|PDB:1P9R"
FT HELIX 377..383
FT /evidence="ECO:0007829|PDB:1P9R"
FT STRAND 384..396
FT /evidence="ECO:0007829|PDB:1P9R"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:1P9R"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:1P9R"
FT HELIX 408..411
FT /evidence="ECO:0007829|PDB:1P9R"
FT STRAND 423..426
FT /evidence="ECO:0007829|PDB:1P9R"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:1P9R"
FT STRAND 435..449
FT /evidence="ECO:0007829|PDB:1P9R"
FT HELIX 452..459
FT /evidence="ECO:0007829|PDB:1P9R"
FT HELIX 464..472
FT /evidence="ECO:0007829|PDB:1P9R"
FT HELIX 478..487
FT /evidence="ECO:0007829|PDB:1P9R"
FT HELIX 493..498
FT /evidence="ECO:0007829|PDB:1P9R"
SQ SEQUENCE 503 AA; 56359 MW; 3FEF661307BB962B CRC64;
MTEMVISPAE RQSIRRLPFS FANRFKLVLD WNEDFSQASI YYLAPLSMEA LVETKRVVKH
AFQLIELSQA EFESKLTQVY QRDSSEARQL MEDIGADSDD FFSLAEELPQ NEDLLESEDD
APIIKLINAM LGEAIKEGAS DIHIETFEKT LSIRFRVDGV LREVLAPSRK LSSLLVSRVK
VMAKLDIAEK RVPQDGRISL RIGGRAVDVR VSTMPSSHGE RVVMRLLDKN ATRLDLHSLG
MTAHNHDNFR RLIKRPHGII LVTGPTGSGK STTLYAGLQE LNSSERNILT VEDPIEFDID
GIGQTQVNPR VDMTFARGLR AILRQDPDVV MVGEIRDLET AQIAVQASLT GHLVMSTLHT
NTAVGAVTRL RDMGIEPFLI SSSLLGVLAQ RLVRTLCPDC KEPYEADKEQ RKLFDSKKKE
PLILYRATGC PKCNHKGYRG RTGIHELLLV DDALQELIHS EAGEQAMEKH IRATTPSIRD
DGLDKVRQGI TSLEEVMRVT KES
