(data stored in ACNUC27125 zone)

HOGENOM: BACPE_1_PE3706

ID   BACPE_1_PE3706                       STANDARD;      PRT;   69 AA.
AC   BACPE_1_PE3706; P22483; D3G0F8;
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; (BACPE_1.PE3706).
GN   Name=atpE; OrderedLocusNames=BpOF4_06875;
OS   BACILLUS PSEUDOFIRMUS OF4.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=398511;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BACPE_1.PE3706.
CC       Bacillus pseudofirmus OF4 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:ATPL_BACPE
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 three main subunits: a(1), b(2) and c(10-14). The alpha and
CC       beta chains form an alternating ring which encloses part of the
CC       gamma chain. F(1) is attached to F(0) by a central stalk formed by
CC       the gamma and epsilon chains, while a peripheral stalk is formed
CC       by the delta and b chains (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the ATPase C chain family.
CC   -!- GENE_FAMILY: HOG000235245 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P22483; D3G0F8; -.
DR   EMBL; AF330160; AAC08039.1; -; Genomic_DNA.
DR   EMBL; CP001878; ADC49433.1; -; Genomic_DNA.
DR   PIR; S17721; S17721.
DR   RefSeq; YP_003426325.1; NC_013791.2.
DR   PDB; 2X2V; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M=1-69.
DR   PDBsum; 2X2V; -.
DR   ProteinModelPortal; P22483; -.
DR   EnsemblBacteria; EBBACT00000287616; EBBACP00000283140; EBBACG00000289637.
DR   GeneID; 8766358; -.
DR   GenomeReviews; CP001878_GR; BpOF4_06875.
DR   KEGG; bpf:BpOF4_06875; -.
DR   GeneTree; EBGT00050000002986; -.
DR   ProtClustDB; PRK06876; -.
DR   GO; GO:0016021; C:integral to 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: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; BACPE_1.PE3706; -.
KW   3D-structure; ATP synthesis; Cell membrane; CF(0); Complete proteome;
KW   Hydrogen ion transport; Ion transport; Lipid-binding; Membrane;
KW   Transmembrane; Transmembrane helix; Transport.
SQ   SEQUENCE   69 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAFLGAAIAA GLAAVAGAIA VAIIVKATIE GTTRQPELRG TLQTLMFIGV PLAEAVPIIA
     IVISLLILF
//

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