ID C5BLP0_TERTT Unreviewed; 514 AA.
AC C5BLP0;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
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:ACR12548.1};
GN OrderedLocusNames=TERTU_0266 {ECO:0000313|EMBL:ACR12548.1};
OS Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Teredinibacter.
OX NCBI_TaxID=377629 {ECO:0000313|EMBL:ACR12548.1, ECO:0000313|Proteomes:UP000009080};
RN [1] {ECO:0000313|EMBL:ACR12548.1, ECO:0000313|Proteomes:UP000009080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39867 / T7901 {ECO:0000313|Proteomes:UP000009080};
RX PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT endosymbiont of marine wood-boring bivalves (shipworms).";
RL PLoS ONE 4:E6085-E6085(2009).
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; CP001614; ACR12548.1; -; Genomic_DNA.
DR RefSeq; WP_015818660.1; NC_012997.1.
DR AlphaFoldDB; C5BLP0; -.
DR STRING; 377629.TERTU_0266; -.
DR KEGG; ttu:TERTU_0266; -.
DR eggNOG; COG2804; Bacteria.
DR HOGENOM; CLU_013446_2_0_6; -.
DR OrthoDB; 9804785at2; -.
DR Proteomes; UP000009080; 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: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:UP000009080};
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"
SQ SEQUENCE 514 AA; 56029 MW; 732824064DAE268A CRC64;
MNVNDEIANE VLSDPLLANA AELEVVEGET AAVMTRFPFS FATNYGVMLH EGRVLHQPGV
SAQTLLEVRR FLGRPFEIEE LDEAAFKARL TRVYQSTDGE ALQAVEDMGA EFDLTALADD
IPDDSELLSG DGDAPVIRLI NAVLSQAVQE KASDIHVEPY EDRVSIRFRV DGILSEVLSP
KPQLAPVLVS RLKVMARLDI AEKRIPQDGR ITVKLAGHAV DIRVSTIPSA HGERVVLRLL
DQAAGQLSLE QLRMPVGVIE TFKGALHKPH GIILVTGPTG SGKTTSLYAG ISHLNSRSRN
ILTVEDPIEY LLPGIGQTQV NTKVDMTFAR GLRAILRQDP DVVMIGEIRD QETASIAVQA
SLTGHLVLST LHTNTAIGAI TRLQDMGVEP FLLSSSLEAL MAQRLVRMLC THCKEETISG
ESELVRLGIP EGSTVFRPVG CDHCHNTGYR GRGGLYEFIQ VDDQLRQLIH EGAGEQVMLA
HARKNSKSID QCGRDKVLSG ETSVEEVLRV TAIS
//
