ID   GSPE_KLEPN              Reviewed;         497 AA.
AC   P15645;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=Pullulanase secretion protein PulE;
DE   AltName: Full=Type II traffic warden ATPase;
GN   Name=pulE;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1738317; DOI=10.1111/j.1365-2958.1992.tb00841.x;
RA   Possot O., d'Enfert C., Reyss I., Pugsley A.P.;
RT   "Pullulanase secretion in Escherichia coli K-12 requires a cytoplasmic
RT   protein and a putative polytopic cytoplasmic membrane protein.";
RL   Mol. Microbiol. 6:95-105(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-149.
RX   PubMed=2677007; DOI=10.1016/s0021-9258(18)71517-2;
RA   D'Enfert C., Reyss I., Wandersman C., Pugsley A.P.;
RT   "Protein secretion by Gram-negative bacteria. Characterization of two
RT   membrane proteins required for pullulanase secretion by Escherichia coli K-
RT   12.";
RL   J. Biol. Chem. 264:17462-17468(1989).
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 PulL/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 PulL/GspL gene product.
CC       {ECO:0000250|UniProtKB:Q00512}.
CC   -!- SIMILARITY: Belongs to the GSP E family. {ECO:0000305}.
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DR   EMBL; M32613; AAA25127.1; -; Genomic_DNA.
DR   PIR; S20034; C34469.
DR   AlphaFoldDB; P15645; -.
DR   SMR; P15645; -.
DR   TCDB; 3.A.15.1.1; the outer membrane protein secreting main terminal branch (mtb) family.
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..497
FT                   /note="Type II secretion system protein E"
FT                   /id="PRO_0000207288"
FT   BINDING         255..262
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         388
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P37093"
FT   BINDING         391
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P37093"
FT   BINDING         419
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P37093"
FT   BINDING         422
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P37093"
SQ   SEQUENCE   497 AA;  55130 MW;  7486926B51728D3B CRC64;
     MTPAAERRPL LPFGYARAHS VMLLSSGESC EVFCLAVTAP QALLEARRVA AMPFRLERLE
     EEAFEKLLVL SYQRDSAEAR RMMADIGNEL DLYTLAEELP DTDDLLDSED DAPIIRLINA
     MLTEAIKEKA SDIHIETYER HLQIRFRVDG VLREILRPQR RLAALLISRI KVMASLDIAE
     KRIPQDGRMA LRIGGRAVDV RVSTLPSSYG ERVVLRLLDK NSVNLDLLTL GMTPALLRQV
     DGLIARPHGI VLVTGPTGSG KSTTLYAALS RLDARERNIM TIEDPIEYEL EGIGQTQVNA
     KVDMTFARGL RAILRQDPDV VLVGEIRDGE TAQIAVQASL TGHLVLSTLH TNSALGAISR
     LQDMGVEPFL LSTSLLAVMS QRLVRRLCPH CRQQEPANAD TAHQMEIAPG TALWQPRGCA
     ECGFTGYRGR TGIHELLLVD DRVRMAIHRG ENEVTLIQQL GTDYMTLRRA GREKALAGIT
     SWQEVLRVTE QPIAEAC