ID   ATPL_HYPNA              Reviewed;          78 AA.
AC   Q0C0X2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=ATP synthase subunit c {ECO:0000255|HAMAP-Rule:MF_01396};
DE   AltName: Full=ATP synthase F(0) sector subunit c {ECO:0000255|HAMAP-Rule:MF_01396};
DE   AltName: Full=F-type ATPase subunit c {ECO:0000255|HAMAP-Rule:MF_01396};
DE            Short=F-ATPase subunit c {ECO:0000255|HAMAP-Rule:MF_01396};
DE   AltName: Full=Lipid-binding protein {ECO:0000255|HAMAP-Rule:MF_01396};
GN   Name=atpE {ECO:0000255|HAMAP-Rule:MF_01396}; OrderedLocusNames=HNE_1920;
OS   Hyphomonas neptunium (strain ATCC 15444).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomonadales;
OC   Hyphomonadaceae; Hyphomonas.
OX   NCBI_TaxID=228405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15444;
RX   PubMed=16980487; DOI=10.1128/jb.00111-06;
RA   Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G.,
RA   Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D.,
RA   Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R.,
RA   Brinkac L.M., Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G.,
RA   Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N.,
RA   Ward N.L.;
RT   "Comparative genomic evidence for a close relationship between the
RT   dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT   crescentus.";
RL   J. Bacteriol. 188:6841-6850(2006).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_01396}.
CC   -!- FUNCTION: Key component of the F(0) channel; it plays a direct role in
CC       translocation across the membrane. A homomeric c-ring of between 10-14
CC       subunits forms the central stalk rotor element with the F(1) delta and
CC       epsilon subunits. {ECO:0000255|HAMAP-Rule:MF_01396}.
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       {ECO:0000255|HAMAP-Rule:MF_01396}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01396}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01396}.
CC   -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000255|HAMAP-
CC       Rule:MF_01396}.
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DR   EMBL; CP000158; ABI77124.1; -; Genomic_DNA.
DR   RefSeq; WP_011646921.1; NC_008358.1.
DR   AlphaFoldDB; Q0C0X2; -.
DR   SMR; Q0C0X2; -.
DR   STRING; 228405.HNE_1920; -.
DR   EnsemblBacteria; ABI77124; ABI77124; HNE_1920.
DR   KEGG; hne:HNE_1920; -.
DR   eggNOG; COG0636; Bacteria.
DR   HOGENOM; CLU_148047_4_0_5; -.
DR   OMA; CMGFCIL; -.
DR   OrthoDB; 2078221at2; -.
DR   Proteomes; UP000001959; 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:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.20.10; -; 1.
DR   HAMAP; MF_01396; ATP_synth_c_bact; 1.
DR   InterPro; IPR000454; ATP_synth_F0_csu.
DR   InterPro; IPR038662; ATP_synth_F0_csu_sf.
DR   InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR   InterPro; IPR035921; F/V-ATP_Csub_sf.
DR   PANTHER; PTHR10031; PTHR10031; 1.
DR   Pfam; PF00137; ATP-synt_C; 1.
DR   PRINTS; PR00124; ATPASEC.
DR   SUPFAM; SSF81333; SSF81333; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Cell inner membrane; Cell membrane; CF(0);
KW   Hydrogen ion transport; Ion transport; Lipid-binding; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..78
FT                   /note="ATP synthase subunit c"
FT                   /id="PRO_1000184397"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
FT   SITE            61
FT                   /note="Reversibly protonated during proton transport"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
SQ   SEQUENCE   78 AA;  7871 MW;  8492470FDE3420CF CRC64;
     MEGNITDGLK YVGAGLATLG MIGSALGVGN IFASFLDAAM RNPSAAPQQT GNLFIGMALA
     EALGIFSVLI AILILFVA