ID   GSPE_PECCC              Reviewed;         498 AA.
AC   P31703;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=Pectic enzymes secretion protein OutE;
DE   AltName: Full=Type II traffic warden ATPase;
GN   Name=outE;
OS   Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp.
OS   carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SCRI 193;
RX   PubMed=8326859; DOI=10.1111/j.1365-2958.1993.tb01589.x;
RA   Reeves P.J., Whitcombe D., Wharam S., Gibson M., Allison G., Bunce N.,
RA   Barallon R., Douglas P., Mulholland V., Stevens S., Walker S.,
RA   Salmond G.P.C.;
RT   "Molecular cloning and characterization of 13 out genes from Erwinia
RT   carotovora subspecies carotovora: genes encoding members of a general
RT   secretion pathway (GSP) widespread in Gram-negative bacteria.";
RL   Mol. Microbiol. 8:443-456(1993).
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 OutL/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 OutL/GspL gene product.
CC       {ECO:0000250|UniProtKB:Q00512}.
CC   -!- SIMILARITY: Belongs to the GSP E family. {ECO:0000305}.
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DR   EMBL; X70049; CAA49646.1; -; Genomic_DNA.
DR   PIR; S32859; S32859.
DR   AlphaFoldDB; P31703; -.
DR   SMR; P31703; -.
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..498
FT                   /note="Type II secretion system protein E"
FT                   /id="PRO_0000207287"
FT   BINDING         261..268
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         394
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P37093"
FT   BINDING         397
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P37093"
FT   BINDING         425
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"
SQ   SEQUENCE   498 AA;  55275 MW;  32ADEB429FC4894B CRC64;
     MSDVASQIIE LRPILPFAYA RSQQILLLQR ENDASLQTIC VAQTPPAALL EARRIAGCSL
     RIERVTDEEF ERQLVISYQR DSEEARRMME DIGNEMDFYT LVEELPDSDD LLDADDDAPI
     IRLINAMLTE AIKNKASDIH IETYERYLLI RFRVDGVLRE ILRPQRKLAS LLVSRIKVMA
     KLDIAEKRVP QDGRMALRVG GRAIDVRVST LPSNYGERVV LRLLDKNSVK LDLELLGMSE
     RNRQLLDSLI HRPHGIILVT GPTGSGKSTT LYAALSRLNA SERNIMTVED PIEYELEGIG
     QTQVNTKVDM TFARGLRAIL RQDPDVVLVG EIRDGETAQI AVQASLTGHL VLSTLHTNSA
     LGALSRLQDM GVEPFLLSTS LLGVLAQRLV RTLCSDCSQP QPVDPVQAEQ MGIAPGTLLH
     NPVGCPQCSF TGYRGRIGIH ELVLINDDVR AAIHRSDGEM AIAQILGGSR TTIRQDGLNK
     VLAGLTTWEE VIRVTKEE