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Database: UniProt
Entry: A0A0E9MMB8_9SPHN
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ID   A0A0E9MMB8_9SPHN        Unreviewed;       518 AA.
AC   A0A0E9MMB8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
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:GAO38684.1};
GN   ORFNames=SCH01S_18_00160 {ECO:0000313|EMBL:GAO38684.1};
OS   Sphingomonas changbaiensis NBRC 104936.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1219043 {ECO:0000313|EMBL:GAO38684.1, ECO:0000313|Proteomes:UP000033202};
RN   [1] {ECO:0000313|EMBL:GAO38684.1, ECO:0000313|Proteomes:UP000033202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 104936 {ECO:0000313|EMBL:GAO38684.1,
RC   ECO:0000313|Proteomes:UP000033202};
RA   Katano-Makiyama Y., Hosoyama A., Hashimoto M., Noguchi M., Tsuchikane K.,
RA   Ohji S., Yamazoe A., Ichikawa N., Kimura A., Fujita N.;
RT   "Whole genome shotgun sequence of Sphingomonas changbaiensis NBRC 104936.";
RL   Submitted (APR-2015) 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:GAO38684.1}.
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DR   EMBL; BBWU01000018; GAO38684.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E9MMB8; -.
DR   STRING; 1219043.SCH01S_18_00160; -.
DR   OrthoDB; 9804785at2; -.
DR   Proteomes; UP000033202; 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   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; 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:UP000033202};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366070};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          336..350
FT                   /note="Bacterial type II secretion system protein E"
FT                   /evidence="ECO:0000259|PROSITE:PS00662"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   518 AA;  54910 MW;  C5587B7679911C9D CRC64;
     MSELHSVPAE AGTLGLRPPP EHSGSAIPIV TVPYAFARKF GVVLLEPDGD RFRVALREGS
     DPRALLEVRR HLGQAMAVES VSAAAFDKLL SDRYALGGEA AAAAAGSLGL GDDLALIAGD
     LPTADDLLDS SDDAPAIRLI NGVIADAVRQ GVSDIHVEPY ESGLIVRMRI DGVLRETLRM
     PAHVAPVLVS RIKVMARLDI AERRVPQDGR ISLMLGGKLL DVRVSTLPSR AGERVVLRIL
     DKENAGLDLA VLGLSPTAEA VLHDALAEPN GIILVTGPTG SGKTTTLYSS LRLLNDGSRN
     ILTVEDPVEY AIEGVGQTQV NPKVGLTFAA GLRAILRQDP DVVMVGEIRD RETAEIAVQA
     SLTGHLVLST VHTNDAVGAI TRMRDMKVEP FLLASTLRAV IAQRLVRRLC PECRLAEPAS
     EQAARLLGLQ PGTIVYEPGG CDACGQTGFR GRVGVFEAVR IDDTIRRLIN EGGDESAIAR
     HAFAKAPSLA AAARALVAAG ETTPEEAVRI TRREQVDA
//
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