GenomeNet

Database: UniProt
Entry: A0A081KDR2_9GAMM
LinkDB: A0A081KDR2_9GAMM
Original site: A0A081KDR2_9GAMM 
ID   A0A081KDR2_9GAMM        Unreviewed;       494 AA.
AC   A0A081KDR2;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
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=GV64_17530 {ECO:0000313|EMBL:KEI72288.1};
OS   Endozoicomonas elysicola.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Endozoicomonadaceae; Endozoicomonas.
OX   NCBI_TaxID=305900 {ECO:0000313|EMBL:KEI72288.1, ECO:0000313|Proteomes:UP000027997};
RN   [1] {ECO:0000313|EMBL:KEI72288.1, ECO:0000313|Proteomes:UP000027997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22380 {ECO:0000313|EMBL:KEI72288.1,
RC   ECO:0000313|Proteomes:UP000027997};
RA   Neave M.J., Apprill A., Voolstra C.R.;
RT   "Whole Genome Sequences of Three Symbiotic Endozoicomonas Bacteria.";
RL   Submitted (JUN-2014) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KEI72288.1}.
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; JOJP01000001; KEI72288.1; -; Genomic_DNA.
DR   RefSeq; WP_026258435.1; NZ_JOJP01000001.1.
DR   AlphaFoldDB; A0A081KDR2; -.
DR   STRING; 305900.GV64_17530; -.
DR   eggNOG; COG2804; Bacteria.
DR   Proteomes; UP000027997; 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: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; 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   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:UP000027997};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366070};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          314..328
FT                   /note="Bacterial type II secretion system protein E"
FT                   /evidence="ECO:0000259|PROSITE:PS00662"
SQ   SEQUENCE   494 AA;  54431 MW;  7D0F81250027A26D CRC64;
     MGEASVLPRL PFTFAKRHGV VLIENDNGVA TLYFHNTPPA DLLAEISRFS GVFPAYQKVN
     VEKLSEVLAH CYHNDSSEAL QNAAGISDHL DLTSLADAVP ITEDLLEQSD DAPVIRLINA
     LLTEAIKEGA SDVHIETFES TLVVRVRIDG VLREILSLQR TIASLLVSRI KVMARLDIAE
     KRVPQDGRIS LRVAGKEVDV RVSTLPSSNG ERVVLRLLDK AAGRLELKHL GMTEQNRSQI
     EYLLKKPYGI ILVTGPTGSG KTTSLYASLT LLNDKTRNIL TVEDPIEYHM EGIGQTQVNT
     KVDMTFARGL RAILRQDPDV VMVGEIRDRE TAEIAVQASL TGHLVLSTLH TNTAVGALTR
     LQDMGIEPFL MSSSLLGVVA QRLVRVLCSE CKSPYSPDDA ECQQLGIRSP EGVTLYHAEG
     CKACNFSGYR GRTGIYEVVV IDEQVRRMIH ALKGEQEITD YVREYSPGIR EDGSRKVLEG
     VTTLEEVLRV TQKD
//
DBGET integrated database retrieval system