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Database: UniProt
Entry: F7NYC8_9GAMM
LinkDB: F7NYC8_9GAMM
Original site: F7NYC8_9GAMM 
ID   F7NYC8_9GAMM            Unreviewed;       502 AA.
AC   F7NYC8;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 46.
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=Rhein_2811 {ECO:0000313|EMBL:EGM77113.1};
OS   Rheinheimera sp. A13L.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Rheinheimera.
OX   NCBI_TaxID=506534 {ECO:0000313|EMBL:EGM77113.1, ECO:0000313|Proteomes:UP000004282};
RN   [1] {ECO:0000313|EMBL:EGM77113.1, ECO:0000313|Proteomes:UP000004282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A13L {ECO:0000313|EMBL:EGM77113.1,
RC   ECO:0000313|Proteomes:UP000004282};
RX   PubMed=21742876; DOI=10.1128/JB.05636-11;
RA   Gupta H.K., Gupta R.D., Singh A., Chauhan N.S., Sharma R.;
RT   "Genome Sequence of Rheinheimera sp. Strain A13L, Isolated from Pangong
RT   Lake, India.";
RL   J. Bacteriol. 193:5873-5874(2011).
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:EGM77113.1}.
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DR   EMBL; AFHI01000026; EGM77113.1; -; Genomic_DNA.
DR   RefSeq; WP_008899653.1; NZ_AFHI01000026.1.
DR   AlphaFoldDB; F7NYC8; -.
DR   STRING; 506534.Rhein_2811; -.
DR   eggNOG; COG2804; Bacteria.
DR   OrthoDB; 9804785at2; -.
DR   Proteomes; UP000004282; 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          321..335
FT                   /note="Bacterial type II secretion system protein E"
FT                   /evidence="ECO:0000259|PROSITE:PS00662"
SQ   SEQUENCE   502 AA;  55504 MW;  129E8E5805782098 CRC64;
     MSAVDLNEMQ PVAAKVRLPF GFAKRFGVLL QAQADGWLLY VNPQTPPAAL LEVRRLLSVS
     FKVQKLQQTE FDALLEASYQ RDSSEAQQIM QDIGNEVDLA SLADEIPETE DLLENEDDAP
     IIKLINAMLG EAIKLGASDI HVETFEKNLV VRFRVDGVLR EVLKPNRKLS SLLVSRIKVM
     AKLDIAEKRV PQDGRISLRI AGRAVDVRVS TMPSSHGERV VMRLLDKNNS HLDLNKLGMT
     PAIQTTFSQL ILKPHGIILV TGPTGSGKST TLYAGLTEIN TKDRNILTVE DPIEYELEGI
     GQTQVNTKVN MTFARGLRAI LRQDPDVVMV GEIRDLETAQ IAVQASLTGH LVLSTLHTNT
     ASGAITRLED MGVEPFLLSS SLLGVLAQRL VRTLCVHCKQ AHEPDKEERA LLGVAKKEGS
     VIYRAIGCEH CNQTGYRGRT GIHELLVVDE HTRELIHNGK GEQSIEKYIR TQGPSIRQDG
     FSKVLTGETT LEEVLRVTRE DL
//
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