ID A0A2H1E6Y5_9FLAO Unreviewed; 62 AA.
AC A0A2H1E6Y5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=ATP synthase F(0) sector subunit c {ECO:0000256|ARBA:ARBA00032200};
DE AltName: Full=F-type ATPase subunit c {ECO:0000256|ARBA:ARBA00032887};
GN Name=atpE {ECO:0000313|EMBL:SFZ80144.1};
GN ORFNames=MARIT_0234 {ECO:0000313|EMBL:SFZ80144.1};
OS Tenacibaculum maritimum NCIMB 2154.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=1349785 {ECO:0000313|EMBL:SFZ80144.1, ECO:0000313|Proteomes:UP000231564};
RN [1] {ECO:0000313|EMBL:SFZ80144.1, ECO:0000313|Proteomes:UP000231564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 2154T {ECO:0000313|EMBL:SFZ80144.1};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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.
CC {ECO:0000256|ARBA:ARBA00025198}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ATPase C chain family.
CC {ECO:0000256|ARBA:ARBA00006704}.
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DR EMBL; LT634361; SFZ80144.1; -; Genomic_DNA.
DR RefSeq; WP_004569351.1; NZ_LT634361.1.
DR AlphaFoldDB; A0A2H1E6Y5; -.
DR STRING; 1349785.GCA_000509405_02417; -.
DR GeneID; 57872894; -.
DR KEGG; tmar:MARIT_0234; -.
DR Proteomes; UP000231564; Chromosome MARIT.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR CDD; cd18121; ATP-synt_Fo_c; 1.
DR Gene3D; 1.20.20.10; F1F0 ATP synthase subunit C; 1.
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; 1.
DR Pfam; PF00137; ATP-synt_C; 1.
DR PRINTS; PR00124; ATPASEC.
DR SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 1.
DR PROSITE; PS00605; ATPASE_C; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310};
KW CF(0) {ECO:0000256|ARBA:ARBA00022547};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Hydrolase {ECO:0000313|EMBL:SFZ80144.1};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000231564};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 43..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..60
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
SQ SEQUENCE 62 AA; 6091 MW; 8969680FFAB70E5E CRC64;
MYNLIGAGLI VIGGGIGLGQ IGGKAMEGIA RQPEAAGKIQ TAMIIIGALL EGLAFGALIL
GK
//
