ID   ATPFD_MYCSK             Reviewed;         443 AA.
AC   A1UJY7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=Mkms_3953;
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=189918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000518; ABL93145.1; -; Genomic_DNA.
DR   RefSeq; WP_011561259.1; NC_008705.1.
DR   AlphaFoldDB; A1UJY7; -.
DR   SMR; A1UJY7; -.
DR   STRING; 189918.Mkms_3953; -.
DR   EnsemblBacteria; ABL93145; ABL93145; Mkms_3953.
DR   KEGG; mkm:Mkms_3953; -.
DR   HOGENOM; CLU_722652_0_0_11; -.
DR   OMA; YVVPPVR; -.
DR   OrthoDB; 1937493at2; -.
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   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; 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..443
FT                   /note="ATP synthase subunit b-delta"
FT                   /id="PRO_0000368894"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..168
FT                   /note="ATP synthase subunit b"
FT   REGION          169..443
FT                   /note="ATP synthase subunit delta"
SQ   SEQUENCE   443 AA;  48270 MW;  FAF6CAFB869089A2 CRC64;
     MSTFIGQLIG FAVIVFLLVR FVVPPVRRMM TAQQETVRRQ LEESSTAANK VAQADQQHAK
     AVEEAKADAR RVVDEARSDA EKIAEQMRAQ ADAEVERIKV QGQAQVQLLR QQLIRELRSH
     LGTESVARAR ELVRDHVSDD DNRSATVDRF LDELDAMAPS DAALDDAVGS RMRSTSRESL
     KALVSRFDEL TADVDADGLT SLGDELAAVA KLLKTEPVLG KHFGEPTEDG EGKANLAEAV
     LSGKISDTAL EVVKAAVAQR WSDESDLDYA VRHTARLALL VRAERNDETS EVEDQLFRFS
     RILDSESRLS GVLSDYTTPV DGRIGLLDRL LGDQAGETTR ALLAQTVELL RGERADEAVR
     ELAELAVARR GEVVAHVNAA AELSDAQRTR LAEVLGRIYG RPASLQLHID PDMLGGLTIA
     VGDEVIDGSL ASRLASAETQ LPD