ATPL_FUSNN
ID ATPL_FUSNN Reviewed; 89 AA.
AC Q8RGD7;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=FN0363;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
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 -!- INTERACTION:
CC Q8RGD7; Q8RGD7: atpE; NbExp=2; IntAct=EBI-16063254, EBI-16063254;
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; AE009951; AAL94566.1; -; Genomic_DNA.
DR RefSeq; NP_603267.1; NC_003454.1.
DR PDB; 3ZK1; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-89.
DR PDB; 3ZK2; X-ray; 2.63 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-89.
DR PDBsum; 3ZK1; -.
DR PDBsum; 3ZK2; -.
DR AlphaFoldDB; Q8RGD7; -.
DR SMR; Q8RGD7; -.
DR DIP; DIP-60173N; -.
DR STRING; 190304.FN0363; -.
DR PRIDE; Q8RGD7; -.
DR EnsemblBacteria; AAL94566; AAL94566; FN0363.
DR KEGG; fnu:FN0363; -.
DR PATRIC; fig|190304.8.peg.940; -.
DR eggNOG; COG0636; Bacteria.
DR HOGENOM; CLU_148047_2_1_0; -.
DR OMA; ALIFRQY; -.
DR BioCyc; FNUC190304:G1FZS-960-MON; -.
DR Proteomes; UP000002521; 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); IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR Gene3D; 1.20.120.610; -; 1.
DR HAMAP; MF_01396; ATP_synth_c_bact; 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; 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.
DR TIGRFAMs; TIGR01260; ATP_synt_c; 1.
DR PROSITE; PS00605; ATPASE_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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..89
FT /note="ATP synthase subunit c"
FT /id="PRO_0000365883"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
FT SITE 65
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
FT HELIX 3..22
FT /evidence="ECO:0007829|PDB:3ZK1"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:3ZK1"
FT HELIX 26..45
FT /evidence="ECO:0007829|PDB:3ZK1"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:3ZK2"
FT HELIX 50..80
FT /evidence="ECO:0007829|PDB:3ZK1"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:3ZK1"
SQ SEQUENCE 89 AA; 8863 MW; 7DD628DF182D3C01 CRC64;
MDLLTAKTIV LGCSAVGAGL AMIAGLGPGI GEGYAAGKAV ESVARQPEAR GSIISTMILG
QAVAESTGIY SLVIALILLY ANPFLSKLG
