ID A0A1C2FZB9_9GAMM Unreviewed; 479 AA.
AC A0A1C2FZB9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=A9R16_15530 {ECO:0000313|EMBL:OCX44622.1};
OS Acidiferrobacter thiooxydans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Acidiferrobacterales;
OC Acidiferrobacteraceae; Acidiferrobacter.
OX NCBI_TaxID=163359 {ECO:0000313|EMBL:OCX44622.1};
RN [1] {ECO:0000313|EMBL:OCX44622.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZJ {ECO:0000313|EMBL:OCX44622.1};
RA Ma L.;
RT "Draft Genome Sequence of Acidiferrobacter thiooxydans ZJ, a Distinctive
RT Species of Ectothiorhodospiraceae.";
RL Submitted (AUG-2016) 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}.
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:OCX44622.1}.
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DR EMBL; MDCF01000175; OCX44622.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C2FZB9; -.
DR STRING; 163359.A9R16_15530; -.
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 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; 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 318..332
FT /note="Bacterial type II secretion system protein E"
FT /evidence="ECO:0000259|PROSITE:PS00662"
SQ SEQUENCE 479 AA; 52401 MW; 95A0AF4FFEB07904 CRC64;
MIERPLDKDW VAKLPYHFAK RYGVMSVGLV GDEVEVWQRA QVPGVVLAEL ERVLRRPLKL
NIVGEEAFLA ALNTGYARDM SQAQQIMGDL DDKLDLAELA QHLPKTQDLL ESEGDAPVVR
LINALLTQAV REQASDIHVE AFETRSLVRF RVDGVLRDVI EPQKAAHGVL VSRIKIMSRL
DIAEKRLPQD GRITLRLAGR PIDVRVSTVP TAHGERVVMR LLDKQAGRLN LGALGMPDDT
LATLRALINE PHGIFLVTGP TGSGKTTTLY SALGELNTHT SNIMTVEDPV EYELDGVGQI
QVNPKIDLTF ARALRSILRQ DPDIVMIGEI RDLETAQIAV QASLTGHLVL ATLHTNDAVG
AVTRLVDMGI EPFLVASTLL GVLAQRLVRT VCGSCHGQAQ STGKSCPACG STGFQGRTGL
YELLTVDDSL KALIHDRAAE ARLREIALSR GLRTLYQDGL RVVAEGRTTT EEVMRVSRD
//
