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Entry: A0Y6N9_9GAMM
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Original site: A0Y6N9_9GAMM 
ID   A0Y6N9_9GAMM            Unreviewed;       521 AA.
AC   A0Y6N9;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 65.
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=ATW7_17487 {ECO:0000313|EMBL:EAW26037.1};
OS   Alteromonadales bacterium TW-7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales.
OX   NCBI_TaxID=156578 {ECO:0000313|EMBL:EAW26037.1, ECO:0000313|Proteomes:UP000004833};
RN   [1] {ECO:0000313|EMBL:EAW26037.1, ECO:0000313|Proteomes:UP000004833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW-7 {ECO:0000313|EMBL:EAW26037.1,
RC   ECO:0000313|Proteomes:UP000004833};
RA   Azam F., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (DEC-2006) 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:EAW26037.1}.
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DR   EMBL; AAVS01000042; EAW26037.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0Y6N9; -.
DR   eggNOG; COG2804; Bacteria.
DR   OrthoDB; 9804785at2; -.
DR   Proteomes; UP000004833; 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          340..354
FT                   /note="Bacterial type II secretion system protein E"
FT                   /evidence="ECO:0000259|PROSITE:PS00662"
SQ   SEQUENCE   521 AA;  57900 MW;  9ECCF1C3FAE27A83 CRC64;
     MTNAIQEINQ DVVHPNTHSA DEPLADDVLV ELPAKRLPFS YARRAGVLLS EYQGQTTVYF
     RGELDLDVLL EVRRIAGHGF KLEQLDDDKF ELLLESSYQR DSSETQQMME DIGNEVDLFS
     LADELPQTED LLAGDDDAPI IKLINAMLSE AIKEGASDIH IETFEQELVI RFRVDGVLKE
     VLKPNRKLAS LLVSRIKVMA KLDIAEKRIP QDGRISLRIA GRAVDVRVST MPSSFGERVV
     LRLLDKNNAR LNLEDLGMTP KNRELFADLI SKPHGIILVT GPTGSGKSTT LYAGMSQINS
     RDRNILTVED PIEYEIPGIG QTQVNTKVDM TFARGLRAIL RQDPDVVMVG EIRDLETAQI
     GVQASLTGHL VMSTLHTNTA SGAITRMEDM GVEPFLLSSS LLGVLSQRLV RTLCNSCKEG
     HVADERECQL LGVPFESKPT IYRAIGCEEC NFNGYKGRTG IHELLVVDET IREMIHNGKG
     EQSVEKYIRT HSPSIRQDGC SRVLAGKTTL EEVLRVTREE G
//
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