GSPE_DICD3
ID GSPE_DICD3 Reviewed; 498 AA.
AC Q01566; E0SM40;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 103.
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; OrderedLocusNames=Dda3937_02416;
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=21217001; DOI=10.1128/jb.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-97.
RC STRAIN=3937;
RX PubMed=1453958; DOI=10.1111/j.1365-2958.1992.tb01775.x;
RA Condemine G., Dorel C., Hugouvieux-Cotte-Pattat N., Robert-Baudouy J.;
RT "Some of the out genes involved in the secretion of pectate lyases in
RT Erwinia chrysanthemi are regulated by kdgR.";
RL Mol. Microbiol. 6:3199-3211(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 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; CP002038; ADM99375.1; -; Genomic_DNA.
DR EMBL; X65265; CAA46371.1; -; Genomic_DNA.
DR PIR; S28015; S28015.
DR RefSeq; WP_013318809.1; NC_014500.1.
DR AlphaFoldDB; Q01566; -.
DR SMR; Q01566; -.
DR STRING; 198628.Dda3937_02416; -.
DR EnsemblBacteria; ADM99375; ADM99375; Dda3937_02416.
DR GeneID; 9734623; -.
DR KEGG; ddd:Dda3937_02416; -.
DR PATRIC; fig|198628.6.peg.3136; -.
DR eggNOG; COG2804; Bacteria.
DR HOGENOM; CLU_013446_2_0_6; -.
DR OMA; RPILPFA; -.
DR OrthoDB; 749544at2; -.
DR BioCyc; DDAD198628:DDA3937_RS14795-MON; -.
DR Proteomes; UP000006859; Chromosome.
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:0016485; P:protein processing; IMP:ASAP.
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; Reference proteome; Translocase;
KW Transport; Zinc.
FT CHAIN 1..498
FT /note="Type II secretion system protein E"
FT /id="PRO_0000207286"
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"
FT CONFLICT 23..24
FT /note="QQ -> HE (in Ref. 2; CAA46371)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 498 AA; 55286 MW; 63864EFD865ADF5C CRC64;
MSDQPVNTPE LRPVLPFSFA RAQQILLLQD ESVTVAEVVC VPDTPALALL EARRVAGVPL
AVSQVSPEEF ERQLVMRYQR DSEEARRLME DIGNDIDFYT LAEELPDSDD LLDGEDDAPI
IRLINAMLTE AIKHKASDIH IETFERHLLI RFRIDGVLRE ILRPQRQLAS LLVSRIKVMA
KLDIAEKRVP QDGRMALRIG GRAIDVRVST LPSNYGERVV LRLLDKNSVR LDLEALGMAE
HNRRQLDTLI HRPHGIILVT GPTGSGKSTT LYAALSRLNS AERNIMTVED PIEYELEGIG
QTQVNPKVDM TFARGLRAIL RQDPDVVLVG EIRDGETAQI AVQASLTGHL VLSTLHTNSA
LGALSRLQDM GIEPFLLSTS LLGVLAQRLV RTLCPSCRQP YVINDEQAQQ TGLAAGTTLY
HPGGCEKCNY SGYRGRTGIH ELLLIDDTVR TAIHHGESEL GIARMLGDKR ITIRQDGLDK
VLAGVTTWEE VVRVTKEE
