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Database: UniProt
Entry: Q3JXR6_BURP1
LinkDB: Q3JXR6_BURP1
Original site: Q3JXR6_BURP1 
ID   Q3JXR6_BURP1            Unreviewed;       497 AA.
AC   Q3JXR6;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   24-JAN-2024, entry version 110.
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=gspE {ECO:0000313|EMBL:ABA47994.1};
GN   OrderedLocusNames=BURPS1710b_0221 {ECO:0000313|EMBL:ABA47994.1};
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372 {ECO:0000313|EMBL:ABA47994.1, ECO:0000313|Proteomes:UP000002700};
RN   [1] {ECO:0000313|EMBL:ABA47994.1, ECO:0000313|Proteomes:UP000002700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b {ECO:0000313|EMBL:ABA47994.1,
RC   ECO:0000313|Proteomes:UP000002700};
RA   Woods D.E., Nierman W.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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|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   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|RuleBase:RU366070}.
CC   -!- SIMILARITY: Belongs to the GSP E family.
CC       {ECO:0000256|ARBA:ARBA00006611, ECO:0000256|RuleBase:RU366070}.
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DR   EMBL; CP000124; ABA47994.1; -; Genomic_DNA.
DR   RefSeq; WP_004196824.1; NC_007434.1.
DR   AlphaFoldDB; Q3JXR6; -.
DR   EnsemblBacteria; ABA47994; ABA47994; BURPS1710b_0221.
DR   GeneID; 56594181; -.
DR   KEGG; bpm:BURPS1710b_0221; -.
DR   HOGENOM; CLU_013446_10_1_4; -.
DR   OMA; QILVAHQ; -.
DR   Proteomes; UP000002700; Chromosome I.
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: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   InterPro; IPR007831; T2SS_GspE_N.
DR   NCBIfam; TIGR02533; type_II_gspE; 1.
DR   PANTHER; PTHR30258:SF2; BACTERIOPHAGE ADSORPTION PROTEIN B; 1.
DR   PANTHER; PTHR30258; TYPE II SECRETION SYSTEM PROTEIN GSPE-RELATED; 1.
DR   Pfam; PF05157; MshEN; 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   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}.
FT   DOMAIN          329..343
FT                   /note="Bacterial type II secretion system protein E"
FT                   /evidence="ECO:0000259|PROSITE:PS00662"
SQ   SEQUENCE   497 AA;  53771 MW;  8E16926710C775C2 CRC64;
     MTQALAQGAP DQPAAGAPSP IAARLLPYGF AKAGQILIAH QHADTLEVWI SERTSSAALA
     EVARNFGAIS LQRMPADELA QAINHAYARQ DGSAAQIVGE VEGEVDLSRL MQDIPEVEDL
     LESEDDAPII RMINALLTQA AREQASDIHI EPFENASVVR FRVDGTLRDV VRPKKALHGA
     LISRIKIMAQ LDIAEKRLPQ DGRITLRVGG RPVDVRVSTL PTGHGERAVL RLLEKDAQRL
     NLEALGMGRD TLVQFDKLIS RPHGIVLVTG PTGSGKTTTL YASMSRLETA TTNIMTVEDP
     IEYDLSGIGQ TQVNERIGMT FARALRSILR QDPDIIMIGE IRDLETAQIA VQASLTGHLV
     LATLHTNDAA SAVTRLTDMG VEPYLLASSL LGVLAQRLVR QLCPACKEER HEGGRAVWHP
     VGCDKCGHSG YTGRRGVYEL LVIDDSIRSL IHRNAADAEI LATGRANGMR TLRDDAERWL
     AAGATSLEEV LRVTGGA
//
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