ID A0A1L8CPK3_9PROT Unreviewed; 463 AA.
AC A0A1L8CPK3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=ATP synthase subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
DE EC=7.1.2.2 {ECO:0000256|HAMAP-Rule:MF_01347};
DE AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
DE AltName: Full=F-ATPase subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
GN Name=atpD {ECO:0000256|HAMAP-Rule:MF_01347};
GN ORFNames=MMIC_P1830 {ECO:0000313|EMBL:GAV20855.1};
OS Mariprofundus micogutta.
OC Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC Mariprofundaceae; Mariprofundus.
OX NCBI_TaxID=1921010 {ECO:0000313|EMBL:GAV20855.1, ECO:0000313|Proteomes:UP000231632};
RN [1] {ECO:0000313|EMBL:GAV20855.1, ECO:0000313|Proteomes:UP000231632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ET2 {ECO:0000313|EMBL:GAV20855.1,
RC ECO:0000313|Proteomes:UP000231632};
RX PubMed=27766355; DOI=10.1007/s00203-016-1307-4;
RA Makita H., Tanaka E., Mitsunobu S., Miyazaki M., Nunoura T., Uematsu K.,
RA Takaki Y., Nishi S., Shimamura S., Takai K.;
RT "Mariprofundus micogutta sp. nov., a novel iron-oxidizing
RT zetaproteobacterium isolated from a deep-sea hydrothermal field at the
RT Bayonnaise knoll of the Izu-Ogasawara arc, and a description of
RT Mariprofundales ord. nov. and Zetaproteobacteria classis nov.";
RL Arch. Microbiol. 199:335-346(2017).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The catalytic sites are hosted primarily by the
CC beta subunits. {ECO:0000256|HAMAP-Rule:MF_01347}.
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:0000256|HAMAP-Rule:MF_01347};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01347};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01347}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_01347}.
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:GAV20855.1}.
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; BDFD01000016; GAV20855.1; -; Genomic_DNA.
DR RefSeq; WP_072660155.1; NZ_BDFD01000016.1.
DR AlphaFoldDB; A0A1L8CPK3; -.
DR STRING; 1921010.MMIC_P1830; -.
DR OrthoDB; 5287966at2; -.
DR Proteomes; UP000231632; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR CDD; cd18110; ATP-synt_F1_beta_C; 1.
DR CDD; cd18115; ATP-synt_F1_beta_N; 1.
DR CDD; cd01133; F1-ATPase_beta_CD; 1.
DR Gene3D; 2.40.10.170; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005722; ATP_synth_F1_bsu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
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 NCBIfam; TIGR01039; atpD; 1.
DR PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF50615; N-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, ECO:0000256|HAMAP-
KW Rule:MF_01347};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01347}; Cell membrane {ECO:0000256|HAMAP-Rule:MF_01347};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|HAMAP-Rule:MF_01347};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP-
KW Rule:MF_01347}; Hydrolase {ECO:0000313|EMBL:GAV20855.1};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_01347};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01347};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01347};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_01347};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01347}.
FT DOMAIN 141..326
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 149..156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01347"
SQ SEQUENCE 463 AA; 50169 MW; C5673E552E2A1339 CRC64;
MSTGTIVQVI GPVVDVRFNA GELPKIYNAL VMQDPKLTME VQQHLGDNTV RAVAMGATDG
LKRGMQLEDT GAAIKVPVGK ATLGRIMNVL GDGIDFEGAD VPSEERWEIH RAAPSFDELS
PAAEILETGI KVIDLMAPIA KGGKVGLFGG AGVGKTVNMM ELINNIAKAH GGFSVFAGVG
ERTREGNDFY YEMKESNVLD KVALVYGQMN EPPGNRLRVA LTGLTMAEYF REDGLDVLIF
IDNIYRYSLA GVEVSALLGR MPSAVGYQPN LAEEMGRLQE RIASTKTGSI TSVQAVYVPA
DDLTDPAPAT TFAHLDSTIV LSRQIAELGI YPAVDPLDST SRQLDPKIIG IEHYEVAQGV
QQTLQRYKEL QDIIAILGMD ELSDEDKLAV QRARKIQRFL SQPFHVAEVF TGSPGVYAKK
DETIKGFKGI LAGEYDHMPE QAFYMVGDIA EAVTKAEKMA AKG
//
