ID A0A160DRK5_9GAMM Unreviewed; 579 AA.
AC A0A160DRK5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-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 ORFNames=I596_751 {ECO:0000313|EMBL:ANB16787.1};
OS Dokdonella koreensis DS-123.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dokdonella.
OX NCBI_TaxID=1300342 {ECO:0000313|EMBL:ANB16787.1, ECO:0000313|Proteomes:UP000076830};
RN [1] {ECO:0000313|EMBL:ANB16787.1, ECO:0000313|Proteomes:UP000076830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-123 {ECO:0000313|EMBL:ANB16787.1,
RC ECO:0000313|Proteomes:UP000076830};
RA Kim J.F., Lee H., Kwak M.-J.;
RT "Complete genome sequence of Dokdonella koreensis DS-123T.";
RL Submitted (APR-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|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; CP015249; ANB16787.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A160DRK5; -.
DR STRING; 1300342.I596_751; -.
DR KEGG; dko:I596_751; -.
DR PATRIC; fig|1300342.3.peg.738; -.
DR Proteomes; UP000076830; 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; 1.10.40.70; -; 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 Reference proteome {ECO:0000313|Proteomes:UP000076830};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366070}.
FT DOMAIN 396..410
FT /note="Bacterial type II secretion system protein E"
FT /evidence="ECO:0000259|PROSITE:PS00662"
SQ SEQUENCE 579 AA; 64565 MW; D8B54E2BE2B6F5D8 CRC64;
MASVIDPAAG VPAVVEETLD ERVCQFLVAR GRLKETDLVR GRRLHEEDNT GSGLLSLLTR
LGLVSERDMA EAMSELMDIA LLPPKEFPET PPPNLQLSVR FLKQVHICPI AETDDEVTLL
IANPADPYPL EAVKLATGRK VQVRLALRSE IDDLIERYYG QGRSAMGTIV ENLSDESGRG
EDDIEHLRDL ASEAPVIRLV NLVIQRAVEQ RASDIHIEPF ENRLKVRYRI DGVLHEVESP
PAASTAAVIS RIKIMAKLNI AERRLPQDGR IMIRVQGKEL DLRVSTVPTA HGESVVMRIL
DREAVVFDFH TLGFTDEFLP KFVKVLEQPH GIMLVTGPTG SGKTTTLYTA LSKLNTPDVK
IITVEDPVEY QIEGINQIQA KPQIGLDFSH ALRSIVRQDP DIIMIGEMRD LETARIAIQS
ALTGHLVLST LHTNNAAGGI TRMLDMGVED YLLTSTINGI LAQRLVRRLD SNTAMPYEAS
PEVIREFNLD RFTDERPIKL YKPMPSPLNS SGYFGRTTIM EFLVMTDALR RQVMQHSTMG
ELEEQARKEG MRTMYEDGIV KSLGGSTTLE EVLRVTQET
//
