ID Q3BXM5_XANC5 Unreviewed; 495 AA.
AC Q3BXM5;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=Type II secretion system protein E {ECO:0000256|RuleBase:RU366070};
DE Short=T2SS protein E {ECO:0000256|RuleBase:RU366070};
DE AltName: Full=Type II traffic warden ATPase {ECO:0000256|RuleBase:RU366070};
GN Name=xcsE {ECO:0000313|EMBL:CAJ22388.1};
GN OrderedLocusNames=XCV0757 {ECO:0000313|EMBL:CAJ22388.1};
OS Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=316273 {ECO:0000313|Proteomes:UP000007069};
RN [1] {ECO:0000313|EMBL:CAJ22388.1, ECO:0000313|Proteomes:UP000007069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=85-10 {ECO:0000313|EMBL:CAJ22388.1,
RC ECO:0000313|Proteomes:UP000007069};
RX PubMed=16237009; DOI=10.1128/JB.187.21.7254-7266.2005;
RA Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneicker S.,
RA Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA Kaiser O.;
RT "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT genome sequence.";
RL J. Bacteriol. 187:7254-7266(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:0000256|ARBA:ARBA00003288, ECO:0000256|RuleBase:RU366070}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC cellular proteinSide 2.; EC=7.4.2.8;
CC Evidence={ECO:0000256|ARBA:ARBA00034006};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004533, ECO:0000256|RuleBase:RU366070}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the GSP E family.
CC {ECO:0000256|ARBA:ARBA00006611, ECO:0000256|RuleBase:RU366070}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM039952; CAJ22388.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3BXM5; -.
DR STRING; 456327.BJD11_19035; -.
DR KEGG; xcv:XCV0757; -.
DR eggNOG; COG2804; Bacteria.
DR HOGENOM; CLU_013446_2_0_6; -.
DR Proteomes; UP000007069; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015627; C:type II protein secretion system complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IEA:UniProtKB-UniRule.
DR CDD; cd01129; PulE-GspE-like; 1.
DR Gene3D; 3.30.450.90; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.300.160; Type II secretion system, protein E, N-terminal domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001482; T2SS/T4SS_dom.
DR InterPro; IPR037257; T2SS_E_N_sf.
DR InterPro; IPR013369; T2SS_GspE.
DR NCBIfam; TIGR02533; type_II_gspE; 1.
DR PANTHER; PTHR30258:SF27; TYPE II SECRETION SYSTEM PROTEIN E-RELATED; 1.
DR PANTHER; PTHR30258; TYPE II SECRETION SYSTEM PROTEIN GSPE-RELATED; 1.
DR Pfam; PF00437; T2SSE; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF160246; EspE N-terminal domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00662; T2SP_E; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU366070};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU366070};
KW Protein transport {ECO:0000256|RuleBase:RU366070};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366070};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 310..324
FT /note="Bacterial type II secretion system protein E"
FT /evidence="ECO:0000259|PROSITE:PS00662"
SQ SEQUENCE 495 AA; 52961 MW; FBDDE2DD75CC935D CRC64;
MSSARASISY AFAKRHGVVL LGSDTTAQIG LREGGDVQAL IELRRALGMP LQVRTLAPSV
FDRHVSEIYA DAGLEQGVQV EALDLHGSLD SLIDDIPTAD LLDSQDDAPI IRLINGIIAE
AARLGASDVH LESYESRLRV RLRVDGVMRE AATLPGRIAP LLVSRVKVMA RLDIAEKRIP
QDGRVSLVMG AKALDVRVST LPTRGSERVV LRILDKEQGT LSLAQLGMPP AVMHTVQRAL
QVPNGIVLVT GPTGSGKTTT LYAALRLLND GSRNILTVED PVEYAIDGVG QTQVNARVGM
TFAAGLRAIL RQDPDVVMIG EIRDTETAQI AVQASLTGHL VLSTVHTNDA VGAVTRLRDM
GIEPFLLASS LRLILAQRLV RRLCPQCRSE RSIDTGTRQL LDAPADAVIY TAVGCNACHH
SGYAGRVGIY EAIAVDDAMR RLIGDNADED ALAAVAFARA PRLGDAARAA VLQGLTTLEE
ALRVTRQQDD AHAAI
//
