ID A0A1E4UTF5_9PSED Unreviewed; 495 AA.
AC A0A1E4UTF5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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 ORFNames=A7D25_21285 {ECO:0000313|EMBL:OEC32998.1};
OS Pseudomonas sp. 21C1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1843690 {ECO:0000313|EMBL:OEC32998.1, ECO:0000313|Proteomes:UP000094259};
RN [1] {ECO:0000313|EMBL:OEC32998.1, ECO:0000313|Proteomes:UP000094259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=21C1 {ECO:0000313|EMBL:OEC32998.1,
RC ECO:0000313|Proteomes:UP000094259};
RA Souza V., Ponce-Soto G.Y.;
RT "Genomic analysis from strains isolated from an enrichment experiment in
RT Cuatro Cienegas.";
RL Submitted (MAY-2016) 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|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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OEC32998.1}.
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; LXJR01000040; OEC32998.1; -; Genomic_DNA.
DR RefSeq; WP_069521736.1; NZ_LXJR01000040.1.
DR AlphaFoldDB; A0A1E4UTF5; -.
DR OrthoDB; 9804785at2; -.
DR Proteomes; UP000094259; Unassembled WGS sequence.
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 InterPro; IPR007831; T2SS_GspE_N.
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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000094259};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366070};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 315..329
FT /note="Bacterial type II secretion system protein E"
FT /evidence="ECO:0000259|PROSITE:PS00662"
SQ SEQUENCE 495 AA; 54543 MW; A9DA26C0E6FBC40E CRC64;
MNASLLKTPL RRLPFSFAKR HGVVLLLEDG QAYVAHRPEV EPVALAEVQR FVGQSLRWRA
LSAAAFEQAL ARAYQHEAGA MQLAEDLGGH LDLTALAEQT PETEDLLEQE DDAPIIRLIN
AILGEAIKED ASDIHLETFE KRLVVRFRVD GMLREVLEPK RGLAALLVSR IKVMARMDIA
EKRVPQDGRI SLKVGGREVD IRVSTLPSAN GERVVLRLLD KQAGRLDLQH LGMSLRDRQV
MEDTVRKPHG ILLVTGPTGS GKTTTLYASL ASLNDRSRNI LTVEDPIEYH LEGIGQTQVN
TKVDMTFARG LRAILRQDPD VVMVGEIRDR ETAEIAVQAS LTGHLVLSTL HTNSAIGAVT
RLVDMGVEPF LLASSLLGVL AQRLVRVLCP ACRQAYQADA AECALLGVDA QNPPTLYRAC
GCAACHQQGY RGRTGIYELV VFDDYLRTLV HSAAAEQVMV RHARTLGPSI RDDGRRKVLE
GVTTVEEVLR VTREE
//
