(data stored in ACNUC27125 zone)

HOGENOM: THMAR2_1_PE164

ID   THMAR2_1_PE164                       STANDARD;      PRT;   81 AA.
AC   THMAR2_1_PE164; E6SLM2;
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;AltName:
DE   Full=Lipid-binding protein;Flags: Precursor; (THMAR2_1.PE164).
GN   Name=atpE; OrderedLocusNames=Tmar_0164;
OS   THERMAEROBACTER MARIANENSIS DSM 12885.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiales Family
OC   XVII. Incertae Sedis; Thermaerobacter.
OX   NCBI_TaxID=644966;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS THMAR2_1.PE164.
CC       Thermaerobacter marianensis DSM 12885 chromosome, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:E6SLM2_THEM7
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       (By similarity).
CC   -!- SIMILARITY: Belongs to the ATPase C chain family.
CC   -!- GENE_FAMILY: HOG000235245 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; E6SLM2; -.
DR   EMBL; CP002344; ADU50289.1; -; Genomic_DNA.
DR   RefSeq; YP_004101016.1; NC_014831.1.
DR   GeneID; 10080534; -.
DR   GenomeReviews; CP002344_GR; Tmar_0164.
DR   KEGG; tmr:Tmar_0164; -.
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: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; 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   HOGENOMDNA; THMAR2_1.PE164; -.
KW   H+transporting two-sector ATPase C subunit;
KW   ATP synthesis; Cell membrane; CF(0); Complete proteome;
KW   Hydrogen ion transport; Ion transport; Lipid-binding; Membrane;
KW   Signal; Transmembrane; Transmembrane helix; Transport.
SQ   SEQUENCE   81 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MEGITGIAFF AGLAVIGLAI AAFGSATGQA RAAAAALDAI WRQPEAAGRI QTVLILSLAF
     LESLTLFTFA LAFLFAGRVA G
//

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