(data stored in ACNUC27125 zone)

HOGENOM: RHBAL1_1_PE2731

ID   RHBAL1_1_PE2731                      STANDARD;      PRT;   88 AA.
AC   RHBAL1_1_PE2731; Q7UH07;
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 1;AltName: Full=ATP synthase F(0)
DE   sector subunit c 1;AltName: Full=F-type ATPase subunit c 1;AltName:
DE   Full=Lipid-binding protein 1; (RHBAL1_1.PE2731).
GN   Name=atpE1; OrderedLocusNames=RB4913;
OS   RHODOPIRELLULA BALTICA SH 1.
OC   Bacteria; Planctomycetes; Planctomycetacia; Planctomycetales;
OC   Planctomycetaceae; Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RHBAL1_1.PE2731.
CC       Rhodopirellula baltica SH 1 chromosome, complete genome.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:Q7UH07_RHOBA
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 inner membrane; Multi-pass membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Belongs to the ATPase C chain family.
CC   -!- GENE_FAMILY: HOG000235245 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q7UH07; -.
DR   EMBL; BX294141; CAD78172.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q7UH07; -.
DR   GenomeReviews; BX119912_GR; RB4913.
DR   KEGG; rba:RB4913; -.
DR   NMPDR; fig|243090.1.peg.2731; -.
DR   OMA; LIFANPF; -.
DR   ProtClustDB; PRK13468; -.
DR   BioCyc; PSP117:RB4913-MONOMER; -.
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:0046933; F:hydrogen ion transporting ATP synthase activity, rotational mechanism; IEA:HAMAP.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; IPR017708; Alt_ATPase_F0-cplx_Csu.
DR   InterPro; IPR000454; ATPase_F0-cplx_csu.
DR   InterPro; IPR005953; ATPase_F0-cplx_csu_bac/chlpt.
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; TIGR03322; Alt_F1F0_F0_C; 1.
DR   TIGRFAMs; TIGR01260; ATP_synt_c; 1.
DR   HOGENOMDNA; RHBAL1_1.PE2731; -.
KW   ATP synthesis; Cell inner membrane; Cell membrane; CF(0);
KW   Complete proteome; Hydrogen ion transport; Hydrolase; Ion transport;
KW   Lipid-binding; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
SQ   SEQUENCE   88 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDSTTSIAVA SIIMAGLTTA IGSIGPAFAE GRAVAQALNS IAQQPDSSNT ITRTLFVGLA
     MIESTAIYCF VVSMILLFAN PFWNQLTQ
//

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