GSPE_PSEAE
ID GSPE_PSEAE Reviewed; 502 AA.
AC Q00512;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Type II secretion system protein E;
DE Short=T2SS protein E;
DE EC=7.4.2.8 {ECO:0000305|PubMed:8102361};
DE AltName: Full=General secretion pathway protein E;
DE AltName: Full=Protein-secreting ATPase;
DE AltName: Full=Type II traffic warden ATPase;
GN Name=xcpR; OrderedLocusNames=PA3103;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=1588814; DOI=10.1111/j.1365-2958.1992.tb01550.x;
RA Bally M., Filloux A., Akrim M., Ball G., Lazdunski A., Tommassen J.;
RT "Protein secretion in Pseudomonas aeruginosa: characterization of seven xcp
RT genes and processing of secretory apparatus components by prepilin
RT peptidase.";
RL Mol. Microbiol. 6:1121-1131(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP GLY-268.
RC STRAIN=PAK;
RX PubMed=8102361; DOI=10.1128/jb.175.16.4962-4969.1993;
RA Turner L.R., Lara J.C., Nunn D.N., Lory S.;
RT "Mutations in the consensus ATP-binding sites of XcpR and PilB eliminate
RT extracellular protein secretion and pilus biogenesis in Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 175:4962-4969(1993).
RN [4]
RP INDUCTION BY LASR-LASI AND RHLR-RHLI.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9218766; DOI=10.1046/j.1365-2958.1997.4271794.x;
RA Chapon-Herve V., Akrim M., Latifi A., Williams P., Lazdunski A., Bally M.;
RT "Regulation of the xcp secretion pathway by multiple quorum-sensing
RT modulons in Pseudomonas aeruginosa.";
RL Mol. Microbiol. 24:1169-1178(1997).
RN [5]
RP SUBUNIT.
RX PubMed=9426126; DOI=10.1046/j.1365-2958.1997.6201986.x;
RA Turner L.R., Olson J.W., Lory S.;
RT "The XcpR protein of Pseudomonas aeruginosa dimerizes via its N-terminus.";
RL Mol. Microbiol. 26:877-887(1997).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GSPL/XCPY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9882649; DOI=10.1128/jb.181.2.382-388.1999;
RA Ball G., Chapon-Herve V., Bleves S., Michel G., Bally M.;
RT "Assembly of XcpR in the cytoplasmic membrane is required for extracellular
RT protein secretion in Pseudomonas aeruginosa.";
RL J. Bacteriol. 181:382-388(1999).
RN [7]
RP INTERACTION WITH XCPY/GSPL; XCPZ/GSPM AND XCPS/GSPF.
RX PubMed=16168578; DOI=10.1016/j.femsle.2005.08.029;
RA Robert V., Filloux A., Michel G.P.;
RT "Subcomplexes from the Xcp secretion system of Pseudomonas aeruginosa.";
RL FEMS Microbiol. Lett. 252:43-50(2005).
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:0000269|PubMed:8102361}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC cellular proteinSide 2.; EC=7.4.2.8;
CC Evidence={ECO:0000305|PubMed:8102361};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P37093};
CC -!- SUBUNIT: Homodimer (PubMed:9426126). Dimerization is directed by a
CC relatively short domain near the extreme N-terminus and is essential
CC for extracellular protein secretion (PubMed:9426126). May form
CC homooligomers (PubMed:9426126). Interacts with XcpY/GspL
CC (PubMed:9882649). Forms an inner membrane platform subcomplex with
CC XcpS/GspF, XcpY/GspL and XcpZ/GspM (PubMed:16168578).
CC {ECO:0000269|PubMed:16168578, ECO:0000269|PubMed:9426126,
CC ECO:0000269|PubMed:9882649}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:9882649}.
CC Note=Membrane association is not an intrinsic property but requires the
CC XcpY/GspL gene product. {ECO:0000269|PubMed:9882649}.
CC -!- INDUCTION: By the two quorum-sensing circuits LasR-LasI and RhlR-RhlI
CC in a growth-phase dependent manner. {ECO:0000269|PubMed:9218766}.
CC -!- DISRUPTION PHENOTYPE: Mutants show complete loss of extracellular
CC exotoxin A secretion. {ECO:0000269|PubMed:8102361}.
CC -!- SIMILARITY: Belongs to the GSP E family. {ECO:0000305}.
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DR EMBL; X62666; CAA44533.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06491.1; -; Genomic_DNA.
DR PIR; S25384; SKPSXR.
DR RefSeq; NP_251793.1; NC_002516.2.
DR RefSeq; WP_003091377.1; NZ_QZGE01000009.1.
DR AlphaFoldDB; Q00512; -.
DR SMR; Q00512; -.
DR STRING; 287.DR97_4830; -.
DR PaxDb; Q00512; -.
DR PRIDE; Q00512; -.
DR EnsemblBacteria; AAG06491; AAG06491; PA3103.
DR GeneID; 877804; -.
DR KEGG; pae:PA3103; -.
DR PATRIC; fig|208964.12.peg.3255; -.
DR PseudoCAP; PA3103; -.
DR HOGENOM; CLU_013446_10_3_6; -.
DR InParanoid; Q00512; -.
DR OMA; RPILPFA; -.
DR PhylomeDB; Q00512; -.
DR BioCyc; PAER208964:G1FZ6-3159-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015627; C:type II protein secretion system complex; IDA:PseudoCAP.
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; IDA:PseudoCAP.
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; Reference proteome; Translocase;
KW Transport; Zinc.
FT CHAIN 1..502
FT /note="Type II secretion system protein E"
FT /id="PRO_0000207289"
FT REGION 461..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 263..270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P37093"
FT BINDING 399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P37093"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P37093"
FT BINDING 432
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P37093"
FT MUTAGEN 268
FT /note="G->S: Complete loss of extracellular alkaline
FT phosphatase or phospholipase C activity."
FT /evidence="ECO:0000269|PubMed:8102361"
SQ SEQUENCE 502 AA; 55525 MW; 3E88B7A95D0C4916 CRC64;
MMTAPLPDIA APAAPPRRLP FSFAKRQGLL FLCLEEQYWL ACRPQVELAA IAEAQRFAGR
RLPLKALGED AFNQALAASY QHDSSAAMQL AEDLGGSLDL AALADQVPET EDLMEQEDDA
PIIRLINAIL GEAIRENASD IHLETFEKRL VVRFRVDGVL REVLEPKREL AALLVSRIKV
MARLDIAEKR IPQDGRISLR VGGREVDIRV STLPSANGER VVLRLLDKQA GRLNLQHLGM
SERDRKLMDE TVRKPHGILL VTGPTGSGKT TTLYASLTTL NDRTRNILTV EDPIEYHLEG
IGQTQVNAKV DMTFARGLRA ILRQDPDVVM VGEIRDRETA EIAVQASLTG HLVLSTLHTN
SAIGAITRLV DMGIEPFLLS SSMLGVLAQR LVRVLCPACK EPYRADEAEC ALLGVDPAAP
PTLHRARGCG ECHQHGYRGR TGIYELVVFD DHMRSLIHNE SSEQEMTRHA RTSGPSIRDD
GRRKVLEGVT TVEEVLRVTR EE
