ID K2E172_9BACT Unreviewed; 335 AA.
AC K2E172;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
DE Flags: Fragment;
GN ORFNames=ACD_22C00216G0001 {ECO:0000313|EMBL:EKD99648.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD99648.1};
RN [1] {ECO:0000313|EMBL:EKD99648.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKD99648.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMFJ01008470; EKD99648.1; -; Genomic_DNA.
DR AlphaFoldDB; K2E172; -.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0006754; P:ATP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 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 {ECO:0000256|ARBA:ARBA00023310};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 19..169
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EKD99648.1"
SQ SEQUENCE 335 AA; 37318 MW; 4D664BAE827AA98E CRC64;
QPLVETGIKV IDLFTPLVKG GKTGLFGGSG VGKTLLLTEI LHNIVNKDKE HNVSVFCGIG
ERTREGHELY RELKKTGVLD HVLLTLSSMG DSSSIRFLTA FSAVTQAEYF RDEMSKDVLF
FIDNIFRFAQ AGNELSLLMN SIPSEDGYQP SLSSEMAAIH ERLVSNKDRS ITTIEAIYMP
ADDLLDQGVQ AVYDYLDSAI VLSRDIYREG RFPAVDILNS TSSSLNLQKV DPVHYYVATK
AQSLLSKAMS LERIVSLVGE SELTDEDRNV YKRALKIKNF MTQNFFVSSE QTGRAGVYVK
LQDTVAGVRR ILDGEMDNIP ENKFMFISTI SDAEK
//
