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Database: UniProt
Entry: Q89AZ7
LinkDB: Q89AZ7
Original site: Q89AZ7 
ID   FLII_BUCBP              Reviewed;         454 AA.
AC   Q89AZ7;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Flagellum-specific ATP synthase;
DE            EC=7.1.2.2;
GN   Name=fliI; OrderedLocusNames=bbp_071;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
CC   -!- FUNCTION: Probable catalytic subunit of a protein translocase for
CC       flagellum-specific export, or a proton translocase involved in local
CC       circuits at the flagellum. May be involved in a specialized protein
CC       export pathway that proceeds without signal peptide cleavage (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10106};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; AE016826; AAO26807.1; -; Genomic_DNA.
DR   RefSeq; WP_011091208.1; NC_004545.1.
DR   AlphaFoldDB; Q89AZ7; -.
DR   SMR; Q89AZ7; -.
DR   STRING; 224915.bbp_071; -.
DR   KEGG; bab:bbp_071; -.
DR   eggNOG; COG1157; Bacteria.
DR   HOGENOM; CLU_022398_5_1_6; -.
DR   OrthoDB; 9148544at2; -.
DR   Proteomes; UP000000601; Chromosome.
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; 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:SF81; FLAGELLUM-SPECIFIC ATP SYNTHASE; 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   3: Inferred from homology;
KW   ATP synthesis; ATP-binding; Bacterial flagellum biogenesis;
KW   Bacterial flagellum protein export; Cytoplasm; Hydrogen ion transport;
KW   Ion transport; Nucleotide-binding; Protein transport; Reference proteome;
KW   Translocase; Transport.
FT   CHAIN           1..454
FT                   /note="Flagellum-specific ATP synthase"
FT                   /id="PRO_0000144692"
FT   BINDING         182..189
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   454 AA;  50559 MW;  2BC512670EBACFDE CRC64;
     MNLRIKKWLE KLDQFEKILV HMPSIMYCGK LIGINGLVLE VSGLKLPIGT ICIVEKNNSI
     LDSDMIEAEV IGFRRNLLLL LLLSNVSDLT ADSKVTPKIL NGSYYNINKL PVCDKLLGRI
     VDGLGKPLDN FSKIDSKYNV SLTNVSINPL HREPVTHVLD TGIRSINGLL TIGRGQKIGL
     FASSGLGKSV LLGMMTRYTQ ADIVILSLIG ERGREVKEFI DSVLTETVLS RSIVISAPSE
     SSVLMQTRGA IYAMRIAEYF RDKNFHVLLI MDSLTRYAMA HREISLSIGE LPVSKGYPPS
     VFSKLFSLIE RAGNGKINSG SITAFFTVLT EEEERYDPIS ESARSILDGH IILSREYAES
     GHYPAINIEN SISRVMPNIV DSSHYSFACH FKKIVSLYQR NRDLINVGAY ISGTDPDLDM
     AITLIPKLNK FLQQGMLEKS NFLDSKKSLY SLFN
//
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