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Database: UniProt
Entry: A0A0W0W3P1_9GAMM
LinkDB: A0A0W0W3P1_9GAMM
Original site: A0A0W0W3P1_9GAMM 
ID   A0A0W0W3P1_9GAMM        Unreviewed;       431 AA.
AC   A0A0W0W3P1;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=protein-secreting ATPase {ECO:0000256|ARBA:ARBA00024382};
DE            EC=7.4.2.8 {ECO:0000256|ARBA:ARBA00024382};
GN   ORFNames=Lisr_1041 {ECO:0000313|EMBL:KTD26830.1};
OS   Legionella israelensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=454 {ECO:0000313|EMBL:KTD26830.1, ECO:0000313|Proteomes:UP000054761};
RN   [1] {ECO:0000313|EMBL:KTD26830.1, ECO:0000313|Proteomes:UP000054761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bercovier 4 {ECO:0000313|EMBL:KTD26830.1,
RC   ECO:0000313|Proteomes:UP000054761};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KTD26830.1}.
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DR   EMBL; LNYH01000052; KTD26830.1; -; Genomic_DNA.
DR   RefSeq; WP_058501402.1; NZ_UGOE01000001.1.
DR   AlphaFoldDB; A0A0W0W3P1; -.
DR   STRING; 454.Lisr_1041; -.
DR   PATRIC; fig|454.4.peg.1121; -.
DR   OrthoDB; 9148544at2; -.
DR   Proteomes; UP000054761; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030257; C:type III protein secretion system complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   GO; GO:0030254; P:protein secretion by the type III secretion system; IEA:InterPro.
DR   CDD; cd01136; ATPase_flagellum-secretory_path_III; 1.
DR   Gene3D; 3.40.50.12240; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR005714; ATPase_T3SS_FliI/YscN.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR040627; T3SS_ATPase_C.
DR   NCBIfam; TIGR01026; fliI_yscN; 1.
DR   PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR   PANTHER; PTHR15184:SF9; SPI-1 TYPE 3 SECRETION SYSTEM ATPASE; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF18269; T3SS_ATPase_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054761};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          151..334
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   431 AA;  47529 MW;  691A5529A805FE63 CRC64;
     MSDVCTSLQS VERLGTIEQV NGLHYVASGP PQVFIGELCE ITNHQHQPLM TAEVTGFNHG
     KVYLMPHSHR PVCMGYPVRA IGKALQIKVS SALLGRIVNA FCQPIDHQGL IKSGESVAIH
     RPPMSPLHRL PVSEQVKTGI HAIDSLMPVG RGQRIGIFAG SGVGKSSLLT MMIQHMQNDI
     NVITFIGERG REVNDFIYHH LSVEETAKKT IVVAACSDES AIIRRQAVYT ATAIAEYFCQ
     KGKNVGLFVD SMTRFAMAQR EIGLSLGEPP TARGYTPSCF SSLPGLIERA GHFQDQGSIT
     GIYTVLVEGD DLNEPVADNM RALLDGHIVL SRQLAQQGCY PAISITESVS RLQNQLFNQE
     ETKIAQDIFS IFSLYQQHLE LIELGAWQKG QNSRLDYAIE RIEALKSIIH QGNSLPLPHT
     DLWKKLMEII S
//
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