ID Q02C61_SOLUE Unreviewed; 449 AA.
AC Q02C61;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=ATPase, FliI/YscN family {ECO:0000313|EMBL:ABJ81355.1};
DE EC=3.6.3.15 {ECO:0000313|EMBL:ABJ81355.1};
GN OrderedLocusNames=Acid_0343 {ECO:0000313|EMBL:ABJ81355.1};
OS Solibacter usitatus (strain Ellin6076).
OC Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC Solibacter.
OX NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ81355.1};
RN [1] {ECO:0000313|EMBL:ABJ81355.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ81355.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Janssen P.H., Kuske C.R., Richardson P.;
RT "Complete sequence of Solibacter usitatus Ellin6076.";
RL Submitted (OCT-2006) 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; CP000473; ABJ81355.1; -; Genomic_DNA.
DR AlphaFoldDB; Q02C61; -.
DR STRING; 234267.Acid_0343; -.
DR KEGG; sus:Acid_0343; -.
DR eggNOG; COG1157; Bacteria.
DR HOGENOM; CLU_022398_5_1_0; -.
DR InParanoid; Q02C61; -.
DR OrthoDB; 9802718at2; -.
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; 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 Hydrolase {ECO:0000313|EMBL:ABJ81355.1};
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 449 AA; 48435 MW; 3940595D27F4E039 CRC64;
MNIDLAPYIS HLDRVNPLRW TGQVTQVVGL LIESRGPSVA IGDFCEVKTA SGRRIHTQVI
GFRDGRVLSM PLEEIDGLQL GDPLAARSED ARVEVGPGLL GRVIDGFGKP MDTGPAINAR
ESYSLHGTPT NPLDRQHITQ PLVTGIRAID ALLPCGKGQR IGIFGGSGVG KSTLLGSMSR
NNSADVTVIA MIGERNREVR GFLENELGPE GRKRSVVVCA TSERPAPLRV RACFVSLAIA
EYFRDQGANV LLVMDSVTRL AMAQREIGLA AGEPPSQKGY TPSVFNLLPK VLERAGNFGR
GSITGFFTVL VEGDDFNEPI CDAVRGILDG HFILSRDLGA QGHYPAIDIL HSVSRLTSAI
ATPAQKEAAR KIRAALAAYR DAEDLIQLGA YVSGSNPDLD ASIHLRPELL DFLRQDHLVV
STLEETLRRL EALATQLQHL PATQAGNKR
//
