ATPB_STRMU
ID ATPB_STRMU Reviewed; 468 AA.
AC P95789;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=ATP synthase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=F-ATPase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
GN Name=atpD {ECO:0000255|HAMAP-Rule:MF_01347};
GN Synonyms=atpB {ECO:0000255|HAMAP-Rule:MF_01347};
GN OrderedLocusNames=SMU_1528;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GS-5;
RX PubMed=8996091; DOI=10.1016/s0378-1119(96)00502-1;
RA Smith A.J., Quivey R.G., Faustoferri R.C.;
RT "Cloning and nucleotide sequence analysis of the Streptococcus mutans
RT membrane-bound, proton-translocating ATPase operon.";
RL Gene 183:87-96(1996).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Smith A.J., Quivey R.G., Faustoferri R.C.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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:0000255|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:0000255|HAMAP-Rule:MF_01347};
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. CF(1) is
CC attached to CF(0) by a central stalk formed by the gamma and epsilon
CC chains, while a peripheral stalk is formed by the delta and b chains.
CC {ECO:0000255|HAMAP-Rule:MF_01347}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01347};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01347}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01347}.
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DR EMBL; U31170; AAD13383.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN59178.1; -; Genomic_DNA.
DR RefSeq; NP_721872.1; NC_004350.2.
DR RefSeq; WP_002262940.1; NC_004350.2.
DR AlphaFoldDB; P95789; -.
DR SMR; P95789; -.
DR STRING; 210007.SMU_1528; -.
DR PRIDE; P95789; -.
DR EnsemblBacteria; AAN59178; AAN59178; SMU_1528.
DR KEGG; smu:SMU_1528; -.
DR PATRIC; fig|210007.7.peg.1360; -.
DR eggNOG; COG0055; Bacteria.
DR HOGENOM; CLU_022398_0_2_9; -.
DR OMA; GFNMIMD; -.
DR PhylomeDB; P95789; -.
DR SABIO-RK; P95789; -.
DR Proteomes; UP000002512; Chromosome.
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: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 Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01039; atpD; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis; ATP-binding; Cell membrane; CF(1); Hydrogen ion transport;
KW Ion transport; Membrane; Nucleotide-binding; Reference proteome;
KW Translocase; Transport.
FT CHAIN 1..468
FT /note="ATP synthase subunit beta"
FT /id="PRO_0000144480"
FT BINDING 155..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT CONFLICT 465
FT /note="N -> K (in Ref. 1; AAD13383)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 50976 MW; 8D6AF6CE782070B5 CRC64;
MSTGKIAQVV GPVVDVAFAT DDKLPEINNA LVVYKDGDKS QRIVLEVALE LGDGLVRTIA
MESTDGLTRG LEVFDTGRAI SVPVGKETLG RVFNVLGDTI DLDKPFAEDA ERQPIHKKAP
SFDDLSTSTE ILETGIKVID LLAPYLKGGK VGLFGGAGVG KTVLIQELIH NIAQEHGGIS
VFTGVGERTR EGNDLYWEMK ESGVIEKTAM VFGQMNEPPG ARMRVALTGL TIAEYFRDVE
GQDVLLFIDN IFRFTQAGSE VSALLGRMPS AVGYQPTLAT EMGQLQERIT STKKGSVTSI
QAIYVPADDY TDPAPATAFA HLDSTTNLER RLTQMGIYPA VDPLASSSRA LSPEIVGQEH
YDVATEVQHV LQRYRELQDI IAILGMDELS DEEKTLVGRA RRIQFFLSQN FNVAEQFTGQ
PGSYVPVAET VRGFKEILEG KYDELPEDAF RSVGAIEDVV EKAKNMGV
