ID B8FMF2_DESAL Unreviewed; 325 AA.
AC B8FMF2;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=ATP synthase subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
DE AltName: Full=ATP synthase F(0) sector subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
DE AltName: Full=F-type ATPase subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
DE Short=F-ATPase subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
DE AltName: Full=Lipid-binding protein {ECO:0000256|HAMAP-Rule:MF_01396};
GN Name=atpE {ECO:0000256|HAMAP-Rule:MF_01396};
GN OrderedLocusNames=Dalk_4310 {ECO:0000313|EMBL:ACL05990.1};
OS Desulfatibacillum aliphaticivorans.
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfatibacillaceae; Desulfatibacillum.
OX NCBI_TaxID=218208 {ECO:0000313|EMBL:ACL05990.1, ECO:0000313|Proteomes:UP000000739};
RN [1] {ECO:0000313|EMBL:ACL05990.1, ECO:0000313|Proteomes:UP000000739}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK-01 {ECO:0000313|EMBL:ACL05990.1,
RC ECO:0000313|Proteomes:UP000000739};
RX PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT for anaerobic alkane oxidation.";
RL Environ. Microbiol. 14:101-113(2012).
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.
CC {ECO:0000256|ARBA:ARBA00025198, ECO:0000256|HAMAP-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:0000256|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:0000256|HAMAP-Rule:MF_01396}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01396}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01396}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ATPase C chain family.
CC {ECO:0000256|ARBA:ARBA00006704, ECO:0000256|HAMAP-Rule:MF_01396}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01396}.
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DR EMBL; CP001322; ACL05990.1; -; Genomic_DNA.
DR RefSeq; WP_015949036.1; NC_011768.1.
DR AlphaFoldDB; B8FMF2; -.
DR KEGG; dal:Dalk_4310; -.
DR eggNOG; COG0636; Bacteria.
DR HOGENOM; CLU_854502_0_0_7; -.
DR Proteomes; UP000000739; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
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 CDD; cd18121; ATP-synt_Fo_c; 4.
DR Gene3D; 1.20.20.10; F1F0 ATP synthase subunit C; 2.
DR Gene3D; 1.20.120.610; lithium bound rotor ring of v- atpase; 1.
DR HAMAP; MF_01396; ATP_synth_c_bact; 4.
DR InterPro; IPR005953; ATP_synth_csu_bac/chlpt.
DR InterPro; IPR000454; ATP_synth_F0_csu.
DR InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
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 NCBIfam; TIGR01260; ATP_synt_c; 2.
DR PANTHER; PTHR10031; ATP SYNTHASE LIPID-BINDING PROTEIN, MITOCHONDRIAL; 1.
DR PANTHER; PTHR10031:SF0; ATPASE PROTEIN 9; 1.
DR Pfam; PF00137; ATP-synt_C; 4.
DR PRINTS; PR00124; ATPASEC.
DR SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 4.
DR PROSITE; PS00605; ATPASE_C; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW Rule:MF_01396}; Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01396};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01396};
KW CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|HAMAP-Rule:MF_01396};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP-
KW Rule:MF_01396};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_01396};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121, ECO:0000256|HAMAP-
KW Rule:MF_01396};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01396};
KW Reference proteome {ECO:0000313|Proteomes:UP000000739};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01396};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01396};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01396}.
FT TRANSMEM 56..79
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01396"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01396"
FT TRANSMEM 137..160
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01396"
FT TRANSMEM 172..197
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01396"
FT TRANSMEM 217..239
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01396"
FT TRANSMEM 251..270
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01396"
FT TRANSMEM 305..324
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01396"
FT DOMAIN 14..77
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
FT DOMAIN 96..158
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
FT DOMAIN 176..239
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
FT DOMAIN 258..321
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
FT SITE 64
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01396"
FT SITE 308
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01396"
SQ SEQUENCE 325 AA; 32328 MW; F7062C5422B9A797 CRC64;
MNDIVMWAEV AAFIGGGLAM GFGAIGAAVG EGYAAANANA AISRNPEVSG DVFKTMLVGQ
AVAESAAIFA LVVAMLLVFA KVDDTATWMT VTVFLSSGLC MGLGAIGSGI GSGFPAGAAC
EGTARQPAMG GRLVTNMLIG SAVCQTPAIF ALVVSFILMF TNFSDRPVNP TWAAILGAGL
ASGLGAIGSG LGGGLVAQAS CEGVARKPEA AGTLTNVMLL GQAVTQTTAI YGMLVSFILM
FKAFDPAGTT LAPAMALLSA GICMGIGAIG PGVGEGFAAQ SAVGWIARNE NATAELTRTM
LVGQAVAEST GIYALVVALV LIFVV
//
