ID A0A0W0XLB0_9GAMM Unreviewed; 429 AA.
AC A0A0W0XLB0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=protein-secreting ATPase {ECO:0000256|ARBA:ARBA00024382};
DE EC=7.4.2.8 {ECO:0000256|ARBA:ARBA00024382};
GN ORFNames=Lqui_2846 {ECO:0000313|EMBL:KTD45375.1};
OS Legionella quinlivanii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45073 {ECO:0000313|EMBL:KTD45375.1, ECO:0000313|Proteomes:UP000054618};
RN [1] {ECO:0000313|EMBL:KTD45375.1, ECO:0000313|Proteomes:UP000054618}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC#1442-AUS-E {ECO:0000313|EMBL:KTD45375.1,
RC ECO:0000313|Proteomes:UP000054618};
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 -!- 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: 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:KTD45375.1}.
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DR EMBL; LNYS01000025; KTD45375.1; -; Genomic_DNA.
DR RefSeq; WP_058508902.1; NZ_UGOX01000001.1.
DR AlphaFoldDB; A0A0W0XLB0; -.
DR STRING; 45073.Lqui_2846; -.
DR PATRIC; fig|45073.5.peg.3022; -.
DR OrthoDB; 9148544at2; -.
DR Proteomes; UP000054618; 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; IPR020003; ATPase_a/bsu_AS.
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.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 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:UP000054618};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 150..332
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 429 AA; 47132 MW; FAF9F72DE9BE3EB2 CRC64;
MKNWSELLQP IERIGEIEQS IGLQLVAKGP PQVFVGETCD ILDSGQQIIT QAEVIGFSQG
KVYLLPFSHT GISMGFKVRA SGHASRIQVG EHLLGKVVNA LAQPLESFIS ASSETLEISG
HAINPMDREM VTEHMITGIH ALDCLIPLGK GQRMGIFAGS GVGKSVLMGM MCRQLQSDIN
VIALVGERGR EVNDFITEHF DEHSRQKSVL VVACSDESAI MRRQAVFTAT AIAEYFCRKG
KQVMLFVDSI TRLAMAQREI GLSLGEPPTS RGYTPSVFAL LPGLVERAGN FIGKGSITGL
YTVLVEGDDF NEPIADTMRS LLDGHIILTR ELAQRGHFPA IDILQSVSRL KDHLLSSSQN
DLVKKVIRLF ALYEQHKDLL ELGGYKAGSN QELDYAIVRI DPLRKLFAQQ KQESLPLSAL
LTRIEEILV
//
