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Database: UniProt
Entry: C3KC61_PSEFS
LinkDB: C3KC61_PSEFS
Original site: C3KC61_PSEFS 
ID   C3KC61_PSEFS            Unreviewed;       472 AA.
AC   C3KC61;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 100.
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   OrderedLocusNames=PFLU_3231 {ECO:0000313|EMBL:CAY49457.1};
OS   Pseudomonas fluorescens (strain SBW25).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=216595 {ECO:0000313|EMBL:CAY49457.1};
RN   [1] {ECO:0000313|EMBL:CAY49457.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SBW25 {ECO:0000313|EMBL:CAY49457.1};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
RN   [2] {ECO:0000313|EMBL:CAI2797447.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SBW25 {ECO:0000313|EMBL:CAI2797447.1};
RA   Fortmann-Grote C.;
RL   Submitted (NOV-2022) 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; OV986001; CAI2797447.1; -; Genomic_DNA.
DR   EMBL; AM181176; CAY49457.1; -; Genomic_DNA.
DR   RefSeq; WP_012724394.1; NC_012660.1.
DR   AlphaFoldDB; C3KC61; -.
DR   STRING; 294.SRM1_03001; -.
DR   PATRIC; fig|216595.4.peg.3397; -.
DR   eggNOG; COG2804; Bacteria.
DR   HOGENOM; CLU_013446_2_0_6; -.
DR   OMA; LIRKPHG; -.
DR   OrthoDB; 9804785at2; -.
DR   Proteomes; UP001152918; Chromosome.
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   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; 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          305..319
FT                   /note="Bacterial type II secretion system protein E"
FT                   /evidence="ECO:0000259|PROSITE:PS00662"
SQ   SEQUENCE   472 AA;  51328 MW;  1F6EA5A35337E591 CRC64;
     MNALPYAWAK AQRILLRNGE EGAVLTVCPS TPGWSISEVR RQFGAARLEQ VRDEELDGLL
     AAAYADTGSA AAVVGAAENE VDLDRLMQDI PEITDLLDTQ DGAPVIRMIN ALLTQAARDE
     ASDIHIEPYE SHSVVRYRVD GTLRDVVSPR KALHAALVSR IKIMAQLDIA EKRLPQDGRI
     ALRVAGRPID IRVSTVPTGH GERVVMRLLD KQAGRLQLET LGMDVQVLAK LDNLIRQPHG
     IVLVTGPTGS GKTTSLYAAL ARLDASTSNI LTVEDPVEYD LPGISQIQVN AKIDMTFALA
     LRAILRQDPD IIMIGEIRDL ETAQIAVQAS LTGHLVLATL HTNDAVSAVN RLIDMGVEPF
     LLASSMLGVL AQRLVRRLCS HCKQEDPAHP GTWRPLGCAA CNHTGYSGRT GIHELFCIDD
     EIRALIHQGA GEQALRLAAR EAGMFSLRED GERWVRAGAT APEEILRVTR DA
//
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