ID T0HU22_9SPHN Unreviewed; 512 AA.
AC T0HU22;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=RLDS_10245 {ECO:0000313|EMBL:EQB15648.1};
OS Sphingobium lactosutens DS20.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1331060 {ECO:0000313|EMBL:EQB15648.1, ECO:0000313|Proteomes:UP000015531};
RN [1] {ECO:0000313|EMBL:EQB15648.1, ECO:0000313|Proteomes:UP000015531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS20 {ECO:0000313|EMBL:EQB15648.1,
RC ECO:0000313|Proteomes:UP000015531};
RX PubMed=24051323;
RA Kumar R., Dwivedi V., Negi V., Khurana J.P., Lal R.;
RT "Draft Genome Sequence of Sphingobium lactosutens Strain DS20T, Isolated
RT from a Hexachlorocyclohexane Dumpsite.";
RL Genome Announc. 1:e00753-13(2013).
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:EQB15648.1}.
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DR EMBL; ATDP01000082; EQB15648.1; -; Genomic_DNA.
DR RefSeq; WP_021225779.1; NZ_ATDP01000082.1.
DR AlphaFoldDB; T0HU22; -.
DR PATRIC; fig|1331060.3.peg.1956; -.
DR eggNOG; COG2804; Bacteria.
DR OrthoDB; 9804785at2; -.
DR Proteomes; UP000015531; 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 Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366070};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 324..338
FT /note="Bacterial type II secretion system protein E"
FT /evidence="ECO:0000259|PROSITE:PS00662"
SQ SEQUENCE 512 AA; 55317 MW; B255D39BE95C7298 CRC64;
MSDLAREEAA PPPPSRPIDI PYVFARKHGV VLLPQDGDRI MIAVRAGSDP RVLLEVRRHL
ARSFDVRFVE PAEFDRHLSN HYAMEGSAAA MAGSLEVGAD ELDILAADIP TADDLLDSAD
DAPAIRLING IIAEAARQGV SDIHIEPYET GLIVRMRVDG VLRETLRMPP HVAPVVVSRI
KVMARLDIAE RRVPQDGRIG LTLGGKLLDV RVSTLPSRAG ERVVLRILDK ENAGMNLDLL
GMTGAPDRIF REGLSEPNGI ILVTGPTGSG KTTTLYAGLR QLNDGSRNIL TVEDPVEYAI
EGVGQTQVNA KVGLTFAAGL RAILRQDPDV VMVGEIRDRE TAEIAVQASL TGHLVLSTVH
TNDAVGAITR MRDMRVEPFL LASTLRAVIA QRLVRRLCQH CREPVQADKS ASALLGFDPG
TIIYKARGCE ECGGSGYKGR IGVFEAIRVD DTIRRLINDG GDESLIARHA FLNAPNLGSA
ARALVRDGQT TAEEAIRVSR RDATEVETIA DG
//
