ID Q9F1Q0_BURCE Unreviewed; 496 AA.
AC Q9F1Q0;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 24-JAN-2024, entry version 86.
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:BAB18789.1};
OS Burkholderia cepacia (Pseudomonas cepacia).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=292 {ECO:0000313|EMBL:BAB18789.1};
RN [1] {ECO:0000313|EMBL:BAB18789.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KF1 {ECO:0000313|EMBL:BAB18789.1};
RA Abe M., Kimoto M., Nakazawa T.;
RT "Molecular organization of the gsp gene cluster in Burkholderia cepacia.";
RL Submitted (OCT-2000) 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; AB050004; BAB18789.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9F1Q0; -.
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 328..342
FT /note="Bacterial type II secretion system protein E"
FT /evidence="ECO:0000259|PROSITE:PS00662"
SQ SEQUENCE 496 AA; 53816 MW; 07B3CDC36D731061 CRC64;
MLASSAHDGA PGERQPPSPL AARLLPYGFA KSGQVLIAHQ LDDTLEVWIS ERTSDAALAE
IARNFGSISV HRVPADELAQ AINQAYARQD GSAAQVVGEV EGEVDLSRLM QDIPEVEDLL
ESEDDAPIIR MINALLTQAA REQASDIHIE PFENASVVRF RVDGTLRDVV RPKKALHGAL
ISRIKIMAQL DIAEKRLPQD GRITLRVGGR PVDVRVSTLP TGHGERAVLR LLEKDAQRLN
LEALGMGRDT LVQFDKLIGR PHGIVLVTGP TGSGKTTTLY ASMSRLETAT TNIMTVEDPI
EYDLSGIGQT QVNERIGMTF ARALRSILRQ DPDVIMIGEI RDLETAQIAV QASLTGHLVL
ATLHTNDAAS AVTRLTDMGV EPYLLASSLL GVLAQRLVRQ LCPVCKEERH EDGRTVWHPV
GCAKCGHSGY AGRRGVYELL VIDDSIRSLI HRNAADAEIL AAGRAEGMRT LRDDAERWLA
SGATSLEEVL RVTGGA
//
