ID   GSPE_AERHY              Reviewed;         501 AA.
AC   P31741;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Type II secretion system protein E;
DE            Short=T2SS protein E;
DE            EC=7.4.2.8 {ECO:0000250|UniProtKB:P37093};
DE   AltName: Full=General secretion pathway protein E;
DE   AltName: Full=Type II traffic warden ATPase;
GN   Name=exeE;
OS   Aeromonas hydrophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Ah65;
RX   PubMed=1640836; DOI=10.1111/j.1365-2958.1992.tb00856.x;
RA   Jiang B., Howard S.P.;
RT   "The Aeromonas hydrophila exeE gene, required both for protein secretion
RT   and normal outer membrane biogenesis, is a member of a general secretion
RT   pathway.";
RL   Mol. Microbiol. 6:1351-1361(1992).
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:0000250|UniProtKB:Q00512}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC         cellular proteinSide 2.; EC=7.4.2.8;
CC         Evidence={ECO:0000250|UniProtKB:P37093};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P37093};
CC   -!- SUBUNIT: Forms homooligomers; most probably hexamers (By similarity).
CC       Interacts with ExeL/GspL (By similarity).
CC       {ECO:0000250|UniProtKB:P37093, ECO:0000250|UniProtKB:Q00512}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:Q00512}. Note=Membrane association is not an
CC       intrinsic property but requires the ExeL/GspL gene product.
CC       {ECO:0000250|UniProtKB:Q00512}.
CC   -!- SIMILARITY: Belongs to the GSP E family. {ECO:0000305}.
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DR   EMBL; X66504; CAA47126.1; -; Genomic_DNA.
DR   PIR; S22669; S22669.
DR   AlphaFoldDB; P31741; -.
DR   SMR; P31741; -.
DR   STRING; 1448139.AI20_16525; -.
DR   PRIDE; P31741; -.
DR   eggNOG; COG2804; Bacteria.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015627; C:type II protein secretion system complex; IEA:InterPro.
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; IEA:InterPro.
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   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane; Metal-binding;
KW   Nucleotide-binding; Protein transport; Translocase; Transport; Zinc.
FT   CHAIN           1..501
FT                   /note="Type II secretion system protein E"
FT                   /id="PRO_0000207283"
FT   BINDING         262..269
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         395
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P37093"
FT   BINDING         398
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P37093"
FT   BINDING         428
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P37093"
FT   BINDING         431
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P37093"
SQ   SEQUENCE   501 AA;  55882 MW;  D8F549B80AA826DE CRC64;
     MAAYQLDDTS LPAALPELPF AFARNFGVVL TERQGTPLLL CRPGVAPQTL LEVRRVAGCA
     FEVEQLGSDE FEELLMAHYQ RDSSEARQLM EDLGNEMDFF ALAEELPQSE DLLDADDDAP
     IIRLINAMLS EAIKEEASDI HIETFERVLV IRFRIDGVLR EILRPHRKLA SLLVSRIKVM
     SRMDIAEKRV PQDGRISLRI GGRAVDVRVS TMPSSYGERV VLRLLDKNNV RLELKQLGMT
     LANRNIISEL IRKPHGIILV TGPTGSGKST TLYAALSEIN SRDRNILTVE DPIEYDLEGV
     GQTQVNTKVD MTFARGLRAI LRQDPDVVMV GEIRDLETAQ IAVQASLTGH LVMSTLHTNT
     AIGAITRMRD MGIEPFLLSS SLLAVLAQRL VRTLCPDCRA PRPITEQERL AMGMELAPDQ
     QVWRPVGCEQ CNHTGYRGRT GIHELVVIDE AVREAIHSAS GELAIERLIR DHTPSIRRDG
     IDKVLKGQTS LEEVLRVTRE D