ID   GSPE_DICCH              Reviewed;         498 AA.
AC   P31702;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 80.
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   Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=EC16;
RX   PubMed=1429461; DOI=10.1128/jb.174.22.7385-7397.1992;
RA   Lindeberg M., Collmer A.;
RT   "Analysis of eight out genes in a cluster required for pectic enzyme
RT   secretion by Erwinia chrysanthemi: sequence comparison with secretion genes
RT   from other Gram-negative bacteria.";
RL   J. Bacteriol. 174:7385-7397(1992).
RN   [2]
RP   INTERACTION WITH OUTL/GSPL; OUTM/GSPM AND OUTF/GSPF.
RX   PubMed=11266368; DOI=10.1093/embo-reports/kve042;
RA   Py B., Loiseau L., Barras F.;
RT   "An inner membrane platform in the type II secretion machinery of Gram-
RT   negative bacteria.";
RL   EMBO Rep. 2:244-248(2001).
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 (PubMed:11266368). Forms an inner membrane
CC       platform subcomplex with OutF/GspF, OutL/GspL and OutM/GspM
CC       (PubMed:11266368). {ECO:0000250|UniProtKB:P37093,
CC       ECO:0000269|PubMed:11266368}.
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; L02214; AAA24832.1; -; Genomic_DNA.
DR   PIR; C47021; C47021.
DR   AlphaFoldDB; P31702; -.
DR   SMR; P31702; -.
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; 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   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   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_0000207285"
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;  55238 MW;  A962852605FCA740 CRC64;
     MSDQPVHTSE LRPVLPFAFA RAQQILLLQD ESASAAEVVC VPETPALALL EVRRVAGVAL
     TVSQVSPEEF ERQLVMRYQR DSEEARRLME DIGNDIDFYT LAEELPDSDD LLDGEDDAPI
     IRLINAMLTE AIKHKASDIH IETFERHLLI RFRIDGVLRE ILRPQRQLAS LLVSRIKVMA
     KLDIAEKRVP QDGRMALRIG GRAIDVRVST LPSNYGERVV LRLLDKNSVR LDLETLGMAE
     HHRRQLDTLI HRPHGIILVT GPTASGKSTT LYAALSPLNS AERNIMTVED PIEYELEGIG
     QTQVNPKVDM TFARGLRAIL RQDPDVVLVG EIRDGETAQI AVQASLTGHL VLSTLHTNSA
     LGALSRLQDM GIEPFLLSTS LLGVLAQRLV RTLCPSCRQP YTIDHEQAEQ TGLAAGTTLY
     HPGGCEKCNY SGYRGRTGIH ELLLIDDTVR AAIHRGESEL GIARMLGAKR VTIRQDGLDK
     VLAGITTWEE VVRVTKEE