ID Q11LM1_CHESB Unreviewed; 465 AA.
AC Q11LM1;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Flagellum-specific ATP synthase {ECO:0000256|ARBA:ARBA00020580};
DE EC=7.1.2.2 {ECO:0000256|ARBA:ARBA00012473};
GN OrderedLocusNames=Meso_0300 {ECO:0000313|EMBL:ABG61704.1};
OS Chelativorans sp. (strain BNC1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Chelativorans.
OX NCBI_TaxID=266779 {ECO:0000313|EMBL:ABG61704.1};
RN [1] {ECO:0000313|EMBL:ABG61704.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BNC1 {ECO:0000313|EMBL:ABG61704.1};
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 Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of chromosome of Chelativorans sp. BNC1.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; CP000390; ABG61704.1; -; Genomic_DNA.
DR AlphaFoldDB; Q11LM1; -.
DR STRING; 266779.Meso_0300; -.
DR KEGG; mes:Meso_0300; -.
DR eggNOG; COG1157; Bacteria.
DR HOGENOM; CLU_022398_5_1_5; -.
DR OrthoDB; 9801639at2; -.
DR GO; GO:0009288; C:bacterial-type flagellum; IEA:InterPro.
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:0044781; P:bacterial-type flagellum organization; IEA:UniProtKB-KW.
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; IPR022426; FliI_clade3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR040627; T3SS_ATPase_C.
DR NCBIfam; TIGR03498; FliI_clade3; 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; 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 Bacterial flagellum biogenesis {ECO:0000256|ARBA:ARBA00022795};
KW Bacterial flagellum protein export {ECO:0000256|ARBA:ARBA00023225};
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 178..362
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 465 AA; 50249 MW; A185FC10512B42D4 CRC64;
MEQSAAENTG PDTAGQANAL AALECVYQRF GDPQRMVRHG GRISEVTPMY YRVRGLSKTA
RLGQIISYRS HGSEYRGEVV RISEDDVIVA PFEHSAEASL GQAVFATGTL EIRPHASWRG
RVIDALARAL DDGPALIRSA PQGPAAMPRT PAALRRQRVA EPFLTGVRVV DLFAPLCLGQ
RIGIFAGSGV GKSTLLAMLA RAEAFDTVVV AMVGERGREV REFLEDTLGE AGMKKTVAVV
ATSDESAMMR RRAADTAMRV AEHFRDAGEK VLLLLDSITR YAHATREVAT GAGEPPVARG
YPASVFTDLP RLLERAGPGE TGHGSITAVF SVLVDGDDHN DPVADCVRGI LDGHLVLDRA
IAEQGRFPAV SPLASISRLA DRSWTDDRKR VVQRLKAMIA RFEETRDIRL LGGFQAGLDP
ELDLAVRQVP LIYDILRQSP KDPPAMDPFA DLAAHLKARE ASHGG
//
