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Database: UniProt
Entry: E1T3W1_BURSG
LinkDB: E1T3W1_BURSG
Original site: E1T3W1_BURSG 
ID   E1T3W1_BURSG            Unreviewed;       526 AA.
AC   E1T3W1;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
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=BC1003_3489 {ECO:0000313|EMBL:ADN59433.1};
OS   Burkholderia sp. (strain CCGE1003).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=640512 {ECO:0000313|EMBL:ADN59433.1};
RN   [1] {ECO:0000313|EMBL:ADN59433.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCGE1003 {ECO:0000313|EMBL:ADN59433.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA   Martinez-Romero E., Rogel M.A., Auchtung J., Tiedje J.M., Woyke T.;
RT   "Complete sequence of chromosome1 of Burkholderia sp. CCGE1003.";
RL   Submitted (SEP-2010) 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; CP002217; ADN59433.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1T3W1; -.
DR   STRING; 640512.BC1003_3489; -.
DR   KEGG; bgf:BC1003_3489; -.
DR   eggNOG; COG2804; Bacteria.
DR   HOGENOM; CLU_013446_10_3_4; -.
DR   OrthoDB; 5790493at2; -.
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   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   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366070}.
FT   DOMAIN          357..371
FT                   /note="Bacterial type II secretion system protein E"
FT                   /evidence="ECO:0000259|PROSITE:PS00662"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   526 AA;  56358 MW;  398984FB974016F9 CRC64;
     MNTPSMPPSA ATSPASSRAA TAPSDGAPAV GSAPAGVAEH AERAAPSAIA ARLVPYGFAR
     SGQILVAHQH ADSLEVWISE RTSEAALAEV ARNFGAVSVV RLPADELAQA INQAYARQDG
     SAAQVVGEVE GEVDLSRLMQ DIPEVEDLLE SEDDAPIIRM INALLTQAAR EQASDIHIEP
     FENASVVRFR VDGTLRDVVR PKKALHGALI SRIKIMAQLD IAEKRLPQDG RITLRVGGRP
     VDVRVSTLPT GHGERAVLRL LEKDAARLNL EALGMGADTL GKFDKLIGRP HGIVLVTGPT
     GSGKTTTLYA SMSRLETATT NIMTVEDPIE YDLSGIGQTQ VNERIGMTFA RALRSILRQD
     PDVIMIGEIR DLETAQIAVQ ASLTGHLVLA TLHTNDAASA VTRLTDMGVE PYLLASSLLG
     VLAQRLVRRL CPVCREQRVD EDGSVHWHPV GCDKCGQSGY AGRRGVYELL LIDDEIRTLI
     HRNASDADIL AAGRAQGMLT LREDAQRWLE SGLTSLEEVI RVTGGA
//
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