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
//