ID A0A1I3BML9_9FIRM Unreviewed; 436 AA.
AC A0A1I3BML9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Flagellum-specific ATP synthase {ECO:0000313|EMBL:SFH63149.1};
GN ORFNames=SAMN04487830_103148 {ECO:0000313|EMBL:SFH63149.1};
OS Pseudobutyrivibrio sp. OR37.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Pseudobutyrivibrio.
OX NCBI_TaxID=1798186 {ECO:0000313|EMBL:SFH63149.1, ECO:0000313|Proteomes:UP000198895};
RN [1] {ECO:0000313|Proteomes:UP000198895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR37 {ECO:0000313|Proteomes:UP000198895};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOQF01000003; SFH63149.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3BML9; -.
DR STRING; 1798186.SAMN04487830_103148; -.
DR Proteomes; UP000198895; 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:0044780; P:bacterial-type flagellum assembly; IEA:InterPro.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro.
DR GO; GO:0030254; P:protein secretion by the type III secretion system; IEA:InterPro.
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; IPR022425; FliI_clade2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR040627; T3SS_ATPase_C.
DR NCBIfam; TIGR03497; FliI_clade2; 1.
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 Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 157..338
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 436 AA; 47377 MW; 5D73D7DC76DBFE46 CRC64;
MDVNSLMQLV EKDYFKSLGK VVKVVGLTIE SVGPEAKLRD LCEIIVEGSH ERIKAEVVGF
KDKRLLLMPY ENVEGIGVGC MVENTGHPLG VAVGNELLGH LVDGLGVPSD VDDLTSFENL
IEYPAEADPP DPMSRVIIKE PLSLGVKAVD GLITVGKGQR IGIFAGSGVG KSTLMGMFAR
NTKAEINVIA LIGERGREVR EFVENDLGPE GMARSVVVCA TSDKPALIRK KAALTATAIA
EYFRDQGRDV LLMMDSLTRF SMAQREIGLA SGEPPVTRGY PPSVYSEMPR LLERAGNSAV
GSITGLYTVL VDGDDFNEPI TDTARSILDG HIMLNRKLAQ KNHYPAIDVL QSISRVMSAV
ATPEHKAIAG KLKNVLATYQ EAEDLINIGA YKNGSNKAID YAIKKIDAVN EFLLQQTHDK
YEFDDIINQM TAIFDD
//