(data stored in ACNUC27125 zone)

HOGENOM: MICAN_1_PE5012

ID   MICAN_1_PE5012                       STANDARD;      PRT;   81 AA.
AC   MICAN_1_PE5012; B0JWU7;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=ATP synthase subunit c;AltName: Full=ATP synthase F(0)
DE   sector subunit c;AltName: Full=F-type ATPase subunit c; Short=F-ATPase
DE   subunit c;AltName: Full=Lipid-binding protein; (MICAN_1.PE5012).
GN   Name=atpE; Synonyms=atpH; OrderedLocusNames=MAE_50120;
OS   MICROCYSTIS AERUGINOSA NIES-843.
OC   Bacteria; Cyanobacteria; Chroococcales; Microcystis.
OX   NCBI_TaxID=449447;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MICAN_1.PE5012.
CC       Microcystis aeruginosa NIES-843, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:ATPL_MICAN
CC   -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the
CC       presence of a proton or sodium gradient. F-type ATPases consist of
CC       two structural domains, F(1) containing the extramembraneous
CC       catalytic core and F(0) containing the membrane proton channel,
CC       linked together by a central stalk and a peripheral stalk. During
CC       catalysis, ATP synthesis in the catalytic domain of F(1) is
CC       coupled via a rotary mechanism of the central stalk subunits to
CC       proton translocation (By similarity).
CC   -!- FUNCTION: Key component of the F(0) channel; it plays a direct
CC       role in translocation across the membrane. A homomeric c-ring of
CC       between 10-14 subunits forms the central stalk rotor element with
CC       the F(1) delta and epsilon subunits (By similarity).
CC   -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic
CC       core - and F(0) - the membrane proton channel. F(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0)
CC       has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha
CC       and beta chains form an alternating ring which encloses part of
CC       the gamma chain. F(1) is attached to F(0) by a central stalk
CC       formed by the gamma and epsilon chains, while a peripheral stalk
CC       is formed by the delta, b and b' chains (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the ATPase C chain family.
CC   -!- GENE_FAMILY: HOG000235245 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B0JWU7; -.
DR   EMBL; AP009552; BAG04834.1; -; Genomic_DNA.
DR   RefSeq; YP_001660026.1; NC_010296.1.
DR   ProteinModelPortal; B0JWU7; -.
DR   STRING; B0JWU7; -.
DR   PRIDE; B0JWU7; -.
DR   GeneID; 5865847; -.
DR   GenomeReviews; AP009552_GR; MAE_50120.
DR   KEGG; mar:MAE_50120; -.
DR   OMA; IGQGNAS; -.
DR   ProtClustDB; PRK07354; -.
DR   BioCyc; MAER449447:MAE_50120-MON; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   HAMAP; MF_01396; ATP_synth_c_bact; 1; -.
DR   InterPro; IPR000454; ATPase_F0-cplx_csu.
DR   InterPro; IPR005953; ATPase_F0-cplx_csu_bac/chlpt.
DR   InterPro; IPR020537; ATPase_F0-cplx_csu_DDCD_BS.
DR   InterPro; IPR002379; ATPase_F0/V0-cplx_csu.
DR   Gene3D; G3DSA:1.20.20.10; ATPase_F0/V0_c; 1.
DR   Pfam; PF00137; ATP-synt_C; 1.
DR   PRINTS; PR00124; ATPASEC.
DR   SUPFAM; SSF81333; ATPase_F0/V0_c; 1.
DR   TIGRFAMs; TIGR01260; ATP_synt_c; 1.
DR   PROSITE; PS00605; ATPASE_C; 1.
DR   HOGENOMDNA; MICAN_1.PE5012; -.
KW   F0F1 ATP synthase subunit C;
KW   ATP synthesis; CF(0); Complete proteome; Hydrogen ion transport;
KW   Ion transport; Lipid-binding; Membrane; Thylakoid; Transmembrane;
KW   Transmembrane helix; Transport.
SQ   SEQUENCE   81 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNPTVAAASV IAAALAVGLA AIGPGVGQGT ASGEAVSGIA RQPEAEGRIR GTLLLSLAFM
     ESLTIYGLVI ALVLLFANPF A
//

If you have problems or comments...

PBIL Back to PBIL home page