GenomeNet

Database: UniProt
Entry: B4WDQ2_9CAUL
LinkDB: B4WDQ2_9CAUL
Original site: B4WDQ2_9CAUL 
ID   B4WDQ2_9CAUL            Unreviewed;       498 AA.
AC   B4WDQ2;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 59.
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=BBAL3_1677 {ECO:0000313|EMBL:EDX80520.1};
OS   Brevundimonas sp. BAL3.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=391600 {ECO:0000313|EMBL:EDX80520.1, ECO:0000313|Proteomes:UP000003957};
RN   [1] {ECO:0000313|EMBL:EDX80520.1, ECO:0000313|Proteomes:UP000003957}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAL3 {ECO:0000313|EMBL:EDX80520.1,
RC   ECO:0000313|Proteomes:UP000003957};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) 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   ---------------------------------------------------------------------------
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; DS989898; EDX80520.1; -; Genomic_DNA.
DR   RefSeq; WP_008261443.1; NZ_DS989898.1.
DR   AlphaFoldDB; B4WDQ2; -.
DR   STRING; 391600.BBAL3_1677; -.
DR   eggNOG; COG2804; Bacteria.
DR   HOGENOM; CLU_013446_2_0_5; -.
DR   OrthoDB; 9804785at2; -.
DR   Proteomes; UP000003957; 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   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366070};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          311..325
FT                   /note="Bacterial type II secretion system protein E"
FT                   /evidence="ECO:0000259|PROSITE:PS00662"
SQ   SEQUENCE   498 AA;  52751 MW;  32ADEA27FD1B561B CRC64;
     MITLVSPSLP YGFAKRHGVL LLDAGEVARV GLREGADPKA LIEARRVLGR PLAVEALSQA
     AFDRQLSEVY AGDHLAATDG DDLDMPAGLD SLIDDIPAAA DLLDTADDAP VIRLINGIIA
     EAVRTGASDI HLETYENALL VRMRIDGVLR EALSLNPRIA PLLVSRIKVM ARLDIAEKRV
     PQDGRIPLAL GGKTLDVRVS TLPSRGGERV VMRILDKDQA GLTLDRLGMA PDALAAFRAA
     LAEPNGIILV TGPTGSGKTT SLYAGLALLN DQTRNILTVE DPVEYAIDGV GQTQVNTKVG
     MTFAAGLRAI LRQDPDVVMV GEIRDVETAG VAVQAALTGH LVLSTVHTND AAGAVTRLRD
     MGVEPFLLAS TLRLIVAQRL VRRLCDHCRT PEIADKKTAK LVGAKAGVQV WRPHGCAHCG
     NTGYVGRVGL YEVLKIDDRV RRLIAAEADE DAVIAAAFAG GGTLTERARA LVLDGVTSVE
     EAVRVARQET ATDPAEAA
//
DBGET integrated database retrieval system