ID B9L6X6_NAUPA Unreviewed; 432 AA.
AC B9L6X6;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Flagellum-specific ATP synthase {ECO:0000313|EMBL:ACM93663.1};
DE EC=3.6.3.14 {ECO:0000313|EMBL:ACM93663.1};
GN OrderedLocusNames=NAMH_1734 {ECO:0000313|EMBL:ACM93663.1};
OS Nautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Nautiliales;
OC Nautiliaceae; Nautilia.
OX NCBI_TaxID=598659 {ECO:0000313|EMBL:ACM93663.1, ECO:0000313|Proteomes:UP000000448};
RN [1] {ECO:0000313|EMBL:ACM93663.1, ECO:0000313|Proteomes:UP000000448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1463 / DSM 18972 / AmH
RC {ECO:0000313|Proteomes:UP000000448};
RX PubMed=19197347; DOI=10.1371/journal.pgen.1000362;
RA Campbell B.J., Smith J.L., Hanson T.E., Klotz M.G., Stein L.Y., Lee C.K.,
RA Wu D., Robinson J.M., Khouri H.M., Eisen J.A., Cary S.C.;
RT "Adaptations to submarine hydrothermal environments exemplified by the
RT genome of Nautilia profundicola.";
RL PLoS Genet. 5:E1000362-E1000362(2009).
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; CP001279; ACM93663.1; -; Genomic_DNA.
DR RefSeq; WP_015902715.1; NC_012115.1.
DR AlphaFoldDB; B9L6X6; -.
DR STRING; 598659.NAMH_1734; -.
DR KEGG; nam:NAMH_1734; -.
DR eggNOG; COG1157; Bacteria.
DR HOGENOM; CLU_022398_5_1_7; -.
DR OrthoDB; 9801639at2; -.
DR Proteomes; UP000000448; 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: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; 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: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.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000313|EMBL:ACM93663.1};
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 154..336
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 432 AA; 47236 MW; D6AF3931661451B0 CRC64;
MALSSIKDKI GKKPLSKPFG IVKKINPTNL IATGLNPSIG DIVKICSGNH EILGMVTALD
ENSFVVTPFS FLEGFKIGDK IYIDENGMQI PVGEGLLGRV VDPFMNPIDD KGDIFFETKY
PIMTKPISPM KRGVINEVFE TKVKAIDGLL TCGKGQKLGI FAGSGVGKST LMSMIVKGAS
ADIKVIALIG ERGREIPEFI EHQLGGDLTN TVIIVATSDD SALMRKYGAF SAMAVAEYFK
DKNKDVLFLM DSITRFAMAQ REIGLAMGEP PTSKGYPPSA IMLLPQLMER AGKEKDKGSI
TAFFTVLVEG DDTSADPIAD QARSILDGHF ILSRELTDSG IYPPINILNS ASRVMNNVVT
KEHLQKAQKF KKLYSLLKEN EVLIRIGAYQ KGVDPELDEA INKKEAMENF LKQSPNELIP
FNETLNLLNN IV
//