ID   ATPFD_MYCPA             Reviewed;         446 AA.
AC   Q73X56;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=MAP_2454c;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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}.
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DR   EMBL; AE016958; AAS04771.1; -; Genomic_DNA.
DR   RefSeq; WP_003873223.1; NC_002944.2.
DR   AlphaFoldDB; Q73X56; -.
DR   SMR; Q73X56; -.
DR   STRING; 262316.MAP_2454c; -.
DR   EnsemblBacteria; AAS04771; AAS04771; MAP_2454c.
DR   KEGG; mpa:MAP_2454c; -.
DR   eggNOG; COG0711; Bacteria.
DR   eggNOG; COG0712; Bacteria.
DR   HOGENOM; CLU_722652_0_0_11; -.
DR   OMA; YVVPPVR; -.
DR   Proteomes; UP000000580; 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.
PE   3: Inferred from homology;
KW   ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport; Ion transport;
KW   Membrane; Multifunctional enzyme; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..446
FT                   /note="ATP synthase subunit b-delta"
FT                   /id="PRO_0000368891"
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;  48538 MW;  6FBDB45E450996BF CRC64;
     MSTFIGQLVG FAAIVFLVVR YVVPPVRRLM AARQEAVRQQ LQDAAAAADR LTESTTAHSK
     AVEAAKAESK RVVDEAQADA KRITEQLAAQ AGLEAERIKS QGSRQVDLLR TQLTRQLRLE
     LGHEAVRQAG ELVRNYVADP AQQSATVDRF LDDLDAMAPA AADVQYPLMT KMRSSSRVAL
     VNLTERFTTV AKDLDNKALS ALSSELVSVA QMLDREIVVT RYLTVPAEDA GPRVRLIERL
     LSGKVGDVTL EVLRAAVSER WSANSDLIDA LEHLSRQALL EVAERENKVD EVEEQLFRFS
     RILDVQPRLA ILLGDYAVPV EGRVGLLRKV LDSASITVNP IVAALLTQTV ELLRGRPAEE
     AVQFLAEVAV ARRGEVVAQV SAAADLSDAQ RSRLTEVLSR IYGHPVSVQL QIDTELLGGL
     LIAVADEVID GTLASRLAAA EAQLPD