GSPE_XANCP
ID GSPE_XANCP Reviewed; 567 AA.
AC P31742;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 3.
DT 03-AUG-2022, entry version 146.
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=Type II traffic warden ATPase;
GN Name=xpsE; Synonyms=pefE; OrderedLocusNames=XCC0660;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=8000 NCPPB 1145;
RX PubMed=1944223; DOI=10.1007/bf00267456;
RA Dums F., Dow J.M., Daniels M.J.;
RT "Structural characterization of protein secretion genes of the bacterial
RT phytopathogen Xanthomonas campestris pathovar campestris: relatedness to
RT secretion systems of other Gram-negative bacteria.";
RL Mol. Gen. Genet. 229:357-364(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Xc1701;
RA Hu N.-T.T., Hung M.-N., Wang K.C.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-149, INTERACTION WITH XPSL, AND
RP MUTAGENESIS OF LEU-40.
RX PubMed=16162504; DOI=10.1074/jbc.m506843200;
RA Chen Y., Shiue S.J., Huang C.W., Chang J.L., Chien Y.L., Hu N.T.,
RA Chan N.L.;
RT "Structure and function of the XpsE N-terminal domain, an essential
RT component of the Xanthomonas campestris type II secretion system.";
RL J. Biol. Chem. 280:42356-42363(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: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 -!- SUBUNIT: Forms homooligomers; most probably hexamers (By similarity).
CC Interacts with XpsL/GspL (PubMed:16162504).
CC {ECO:0000250|UniProtKB:P37093, ECO:0000269|PubMed:16162504}.
CC -!- INTERACTION:
CC P31742; P31742: xpsE; NbExp=2; IntAct=EBI-8167266, EBI-8167266;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:Q00512}. Note=Membrane association is not an
CC intrinsic property but requires the XpsL/GspL gene product.
CC {ECO:0000250|UniProtKB:Q00512}.
CC -!- SIMILARITY: Belongs to the GSP E family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM39976.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA41803.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X59079; CAA41803.1; ALT_INIT; Genomic_DNA.
DR EMBL; L02630; AAC27375.4; -; Genomic_DNA.
DR EMBL; AE008922; AAM39976.1; ALT_INIT; Genomic_DNA.
DR PIR; S17937; S17937.
DR PIR; T12056; T12056.
DR RefSeq; NP_636052.1; NC_003902.1.
DR PDB; 2D27; X-ray; 2.21 A; A=1-149.
DR PDB; 2D28; X-ray; 2.00 A; C=1-149.
DR PDBsum; 2D27; -.
DR PDBsum; 2D28; -.
DR AlphaFoldDB; P31742; -.
DR SMR; P31742; -.
DR IntAct; P31742; 1.
DR MINT; P31742; -.
DR STRING; 340.xcc-b100_3695; -.
DR EnsemblBacteria; AAM39976; AAM39976; XCC0660.
DR KEGG; xcc:XCC0660; -.
DR PATRIC; fig|190485.4.peg.724; -.
DR eggNOG; COG2804; Bacteria.
DR HOGENOM; CLU_013446_10_6_6; -.
DR OMA; QAGMRTM; -.
DR BRENDA; 7.4.2.8; 6708.
DR EvolutionaryTrace; P31742; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015627; C:type II protein secretion system complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; IBA:GO_Central.
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 InterPro; IPR007831; T2SS_GspE_N.
DR Pfam; PF00437; T2SSE; 1.
DR Pfam; PF05157; T2SSE_N; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Protein transport; Reference proteome; Translocase;
KW Transport.
FT CHAIN 1..567
FT /note="Type II secretion system protein E"
FT /id="PRO_0000207291"
FT BINDING 325..332
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 40
FT /note="L->D: Complete loss of interaction with XpsL."
FT /evidence="ECO:0000269|PubMed:16162504"
FT CONFLICT 88
FT /note="L -> V (in Ref. 1; CAA41803)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="Q -> H (in Ref. 2; AAC27375)"
FT /evidence="ECO:0000305"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:2D28"
FT HELIX 22..27
FT /evidence="ECO:0007829|PDB:2D28"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:2D28"
FT HELIX 51..62
FT /evidence="ECO:0007829|PDB:2D28"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:2D28"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2D27"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:2D28"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:2D28"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:2D28"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:2D28"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:2D28"
FT HELIX 137..147
FT /evidence="ECO:0007829|PDB:2D28"
SQ SEQUENCE 567 AA; 63144 MW; 19B0E31CF14081FD CRC64;
MEQRSAETRI VEALLERRRL KDTDLVRARQ LQAESGMGLL ALLGRLGLVS ERDHAETCAE
VLGLPLVDAR QLGDTPPEML PEVQGLSLRF LKQFHLCPVG ERDGRLDLWI ADPYDDYAID
AVRLATGLPL LLQVGLRSEI DDLIERWYGQ GRSAMGTIVE TADGDASSTD DIEALRDLAS
EAPVIRLVNL VIQHAVELRA SDIHIEPFES RLKVRYRVDG VLVEGESPPA KLTAAVISRI
KIMAKLNIAE RRLPQDGRIM LRVQGKELDL RVSTVPTAHG ESVVMRLLDR ETVVFDFYKL
GFTEDFLPQF RKVLEQPHGI MLVTGPTGSG KTTTLYTALS QLNTSDVKII TVEDPVEYQI
EGINQIQAKP QIGLDFANAL RSIVRQDPDI IMIGEMRDLE TARIAIQSAL TGHLVLSTLH
TNNAAGGITR LLDMGVEDYL LTSTINGILA QRLVRKLDLA NAERYAASPE EIERFDLRRL
QPDGEIFLYR PRATAAAPTG YLGRTTIVEF LVMNDELRRA VMRRAGMGEI EQLARKSGMR
TMYEDGLSKA LRGETTIEEV LRVTEDA
