ID   ATPB_MALP2              Reviewed;         778 AA.
AC   Q8EWY8;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=ATP synthase subunit beta;
DE            EC=7.1.2.2;
DE   AltName: Full=ATP synthase F1 sector subunit beta;
DE   AltName: Full=F-ATPase subunit beta;
GN   Name=atpD; OrderedLocusNames=MYPE620;
OS   Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans).
OC   Bacteria; Tenericutes; Mycoplasmoidales; Mycoplasmoidaceae; Malacoplasma.
OX   NCBI_TaxID=272633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HF-2;
RX   PubMed=12466555; DOI=10.1093/nar/gkf667;
RA   Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K.,
RA   Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.;
RT   "The complete genomic sequence of Mycoplasma penetrans, an intracellular
RT   bacterial pathogen in humans.";
RL   Nucleic Acids Res. 30:5293-5300(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 (By 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   -!- 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       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; BA000026; BAC43852.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8EWY8; -.
DR   SMR; Q8EWY8; -.
DR   STRING; 272633.26453520; -.
DR   EnsemblBacteria; BAC43852; BAC43852; BAC43852.
DR   KEGG; mpe:MYPE620; -.
DR   eggNOG; COG0055; Bacteria.
DR   HOGENOM; CLU_359749_0_0_14; -.
DR   Proteomes; UP000002522; 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..778
FT                   /note="ATP synthase subunit beta"
FT                   /id="PRO_0000254307"
FT   REGION          1..289
FT                   /note="Unknown"
FT   REGION          290..778
FT                   /note="ATP synthase subunit beta"
FT   BINDING         447..454
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   778 AA;  87811 MW;  C4BB48646C2BBC6B CRC64;
     MKENNKTIEA KNKELRDATK EFNEKLQKFL KDKVKKGFQI KNPNYKIDDN KISSNEVFKN
     NKNDFELNLP KNTWEEKTNK PESFENYKNV IPPYEDKFLP ENFKEKFAPK NIKSEPLINK
     KDNLKEKNNN PVFDEVKIQE DDKFFDFSKF SETVSNQPEN ILKIEENDFK EIHDDFVSQY
     ETFSKLETKE NTNDLKTNLS SDTIKTIESK NEPEVQIESE IKDDSLEKEI SEDDSFMDIF
     KAEQPDNQED DSFVIDEEKA KEEYQEIKTN KSIVSDSHKI DIYEENEDLM KLNTLKSDKG
     IIYQIFGPVV DVKFARNQMP NINDCLEVKL PNNKKLVLEV ALLEGDDVAR CISMGSTEGL
     YRGLEVINTK NPIMAPVGSA VLGRMFNVVG EPIDNKPMPE KVEYSPIHKK PPSFDEQSTK
     TEIFETGIKV IDLLVPYVKG GKIGLFGGAG VGKTVLVQEL IHNIATGHGG LSIFAGVGER
     TREGNDLYHE MIDGGVINQT ALVFGQMNEP PGARMRVALT ALTMAEHFRE NNKQDVLLFI
     DNIFRFSQAG SEVSALLGRI PSAVGYQPTL AFEMGQLQER ITSTKSGSIT SVQAVYVPAD
     DLTDPAPSTT FAHLDAKTVL DRKIASLGIY PAINPLESSS RMLDPSIVGI EHYKVARSVQ
     TILQKFEELQ DIIAILGIDE LSEEDKLTVS RARKIRNFLS QPFFVAEKFS HKSGKYVSTQ
     DTISGFSEII EGKCDDIPEQ YFLYVGGIDD VHKNYVAANS NNKVNSSNKP LNSENKSN