ID   ATPFD_MYCBP             Reviewed;         446 AA.
AC   A1KI95;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=ATP synthase subunit b-delta;
DE   Includes:
DE     RecName: Full=ATP synthase subunit b;
DE     AltName: Full=ATP synthase F(0) sector subunit b 2;
DE     AltName: Full=ATPase subunit I 2;
DE     AltName: Full=F-type ATPase subunit b 2;
DE              Short=F-ATPase subunit b 2;
DE   Includes:
DE     RecName: Full=ATP synthase subunit delta;
DE     AltName: Full=ATP synthase F(1) sector subunit delta;
DE     AltName: Full=F-type ATPase subunit delta;
DE              Short=F-ATPase subunit delta;
GN   Name=atpFH; Synonyms=atpF, atpH; OrderedLocusNames=BCG_1367;
OS   Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=410289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Pasteur 1173P2;
RX   PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA   Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA   Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA   Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA   Barrell B.G., Parkhill J., Cole S.T.;
RT   "Genome plasticity of BCG and impact on vaccine efficacy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
CC   -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC       of a proton or sodium gradient. F-type ATPases consist of two
CC       structural domains, F(1) containing the extramembraneous catalytic core
CC       and F(0) containing the membrane proton channel, linked together by a
CC       central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC       in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC       the central stalk subunits to proton translocation (By similarity).
CC       {ECO:0000250}.
CC   -!- FUNCTION: This fusion protein includes a component of the F(0) channel
CC       (subunit b) and of the F(1) subunit (subunit delta). Two copies of
CC       subunit b and one of delta together form the peripheral 'stator' stalk
CC       which links F(1) to F(0) (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC       - and F(0) - the membrane proton channel. F(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main
CC       subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an
CC       alternating ring which encloses part of the gamma chain. F(1) is
CC       attached to F(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}; Single-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the ATPase B chain
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the ATPase delta
CC       chain family. {ECO:0000305}.
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; AM408590; CAL71354.1; -; Genomic_DNA.
DR   RefSeq; WP_003406697.1; NC_008769.1.
DR   AlphaFoldDB; A1KI95; -.
DR   SMR; A1KI95; -.
DR   GeneID; 45425281; -.
DR   KEGG; mbb:BCG_1367; -.
DR   HOGENOM; CLU_722652_0_0_11; -.
DR   OMA; YVVPPVR; -.
DR   Proteomes; UP000001472; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.520.20; -; 1.
DR   HAMAP; MF_01398; ATP_synth_b_bprime; 1.
DR   HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR   InterPro; IPR028987; ATP_synth_B-like_membr_sf.
DR   InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR   InterPro; IPR005864; ATP_synth_F0_bsu_bac.
DR   InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf.
DR   InterPro; IPR000711; ATPase_OSCP/dsu.
DR   PANTHER; PTHR11910; PTHR11910; 1.
DR   Pfam; PF00430; ATP-synt_B; 1.
DR   Pfam; PF00213; OSCP; 1.
DR   PRINTS; PR00125; ATPASEDELTA.
DR   SUPFAM; SSF81573; SSF81573; 1.
DR   TIGRFAMs; TIGR01144; ATP_synt_b; 1.
DR   TIGRFAMs; TIGR01145; ATP_synt_delta; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport; Ion transport;
KW   Membrane; Multifunctional enzyme; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..446
FT                   /note="ATP synthase subunit b-delta"
FT                   /id="PRO_0000368888"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..168
FT                   /note="ATP synthase subunit b"
FT   REGION          169..446
FT                   /note="ATP synthase subunit delta"
SQ   SEQUENCE   446 AA;  48806 MW;  AF07F26E38B78315 CRC64;
     MSTFIGQLFG FAVIVYLVWR FIVPLVGRLM SARQDTVRQQ LADAAAAADR LAEASQAHTK
     ALEDAKSEAH RVVEEARTDA ERIAEQLEAQ ADVEAERIKM QGARQVDLIR AQLTRQLRLE
     LGHESVRQAR ELVRNHVADQ AQQSATVDRF LDQLDAMAPA TADVDYPLLA KMRSASRRAL
     TSLVDWFGTM AQDLDHQGLT TLAGELVSVA RLLDREAVVT RYLTVPAEDA TPRIRLIERL
     VSGKVGAPTL EVLRTAVSKR WSANSDLIDA IEHVSRQALL ELAERAGQVD EVEDQLFRFS
     RILDVQPRLA ILLGDCAVPA EGRVRLLRKV LERADSTVNP VVVALLSHTV ELLRGQAVEE
     AVLFLAEVAV ARRGEIVAQV GAAAELSDAQ RTRLTEVLSR IYGHPVTVQL HIDAALLGGL
     SIAVGDEVID GTLSSRLAAA EARLPD