ID A0A0P6WXP7_9CHLR Unreviewed; 446 AA.
AC A0A0P6WXP7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=ATP synthase {ECO:0000313|EMBL:KPL71099.1};
GN ORFNames=ADM99_12570 {ECO:0000313|EMBL:KPL71099.1};
OS Leptolinea tardivitalis.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Leptolinea.
OX NCBI_TaxID=229920 {ECO:0000313|EMBL:KPL71099.1, ECO:0000313|Proteomes:UP000050430};
RN [1] {ECO:0000313|EMBL:KPL71099.1, ECO:0000313|Proteomes:UP000050430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YMTK-2 {ECO:0000313|EMBL:KPL71099.1,
RC ECO:0000313|Proteomes:UP000050430};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Genome sequence of Leptolinea tardivitalis DSM 16556.";
RL Submitted (JUL-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:KPL71099.1}.
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DR EMBL; LGCK01000012; KPL71099.1; -; Genomic_DNA.
DR RefSeq; WP_062422846.1; NZ_LGCK01000012.1.
DR AlphaFoldDB; A0A0P6WXP7; -.
DR STRING; 229920.ADM99_12570; -.
DR PATRIC; fig|229920.5.peg.2838; -.
DR OrthoDB; 9802718at2; -.
DR Proteomes; UP000050430; 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; cd18114; ATP-synt_flagellum-secretory_path_III_C; 1.
DR CDD; cd18117; ATP-synt_flagellum-secretory_path_III_N; 1.
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; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
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; PF02874; ATP-synt_ab_N; 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:UP000050430};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 161..342
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 446 AA; 47956 MW; 8617A23990E1629A CRC64;
MNQVNPVDFS PLLRSLDNCN ALRVSGRVVQ VIGLTIEAVG LDCQIGEVCE IRARSGEKIL
SEVVGFRNST TLLMPLGNME GIQPDSSIYP QKTVLRAPVG SQLLGRVLDG LGEPIDGNGP
LGEVETRPIN NAAPHPMERQ IITEPLVTGV RAIDGFLTCG KGQRMGIFAG SGVGKSTLMG
SIARSSHSDV SVIALIGERG REVRDFVEGD LGKEGLERSV VVVSTSDKPA LMRLKAAYVA
MTIAEDFRDQ GMDVTFLMDS VTRFAMAQRE VGLAIGEPPA SRGYTPSVFA LLPKLLERAG
TGQRGSITGY FTVLVEGDDF NEPICDAVRS ILDGHIILSR QLATRNHYPA IDVLGSISRV
MPHITSREHR SWAAKARRLL ATYEKARDLI NIGAYVAGSD PEVDEAISAM PIIDSFLLQG
KEFSEFSETL SQLESIGGEI GVDHAA
//
