SPM_004535


  Uniprot: A0A037UP98
Description: ATP F0F1 synthase subunit delta
EC number: 
Annotation score: 2 out of 5
Miscellaneous [CC]: 
Protein existence: Inferred from homology
Catalytic activity: 
Cofactor: 
Enzyme regulation: 
Function [CC]: FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. {ECO:0000256|HAMAP-Rule:MF_01416}.; FUNCTION: This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. {ECO:0000256|HAMAP-Rule:MF_01416}.
Pathway: 
Active site: 
Binding site: 
Calcium binding: 
DNA binding: 
Metal binding: 
Nucleotide binding: 
Site: 
Gene names (primary): atpH
Gene names (synonym): 
Mass: 21,053
Subunit structure [CC]: 
Gene ontology (GO): plasma membrane [GO:0005886]; proton-transporting ATP synthase complex, catalytic core F(1) [GO:0045261]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]; plasma membrane ATP synthesis coupled proton transport [GO:0042777]
Gene ontology IDs: GO:0005886; GO:0042777; GO:0045261; GO:0046933
Chain: 
Signal peptide: 
Domain [CC]: 
Sequence similarities: SIMILARITY: Belongs to the ATPase delta chain family. {ECO:0000256|HAMAP-Rule:MF_01416}.
Protein families: ATPase delta chain family
Coiled coil: 
Domain [FT]: 
Motif: 
Region: 
EMBL: AGBZ02000003
ProteinModelPortal: 
MEROPS: 
EnsemblBacteria KO: KAI92438
UniPathway: 
CDD: 
Gene3D: 
HAMAP: 1.10.520.20
InterPro: MF_01416
PANTHER: IPR026015;IPR000711
PIRSF: PTHR11910
PRINTS: 
PROSITE: PR00125
Pfam: 
ProDom: PF00213
SMART: 
SUPFAM: 
TIGRFAMs: SSF47928
66128-66674(-)

>nucleotide sequence
CTATTTATTATGTATTGCTTTTTGTCGCATTGTTTCTAATTGTCCTGCAATTGAACCATC
AATAATTTCGTGCTTAATTTTAATTCGAACTCCGCCTAATAAAGATGAATCAATTTTGTT
AACTAACTCAATATGATAACCAAATTTTTTACTTAATTTTGTTTCAATTGTTGTAATTTG
TTTTTTTGTTAATGGTTGTGTTGAATAAATATTTCCATATTGAACATCATAACTAATATT
AATTAGTTTTCTTAACCGTTTAAAAATTCTTCTAACATAGCAAAAAGCTTCGCGATCAAT
TAATAAAAAAAGGGCATTTAAAATTAATGGATCAATAACTTTTTGAAATGGTTTTGCTAA
AATATTCTTTCGTTCTTCTTTTGGAATGTCAGCATTCATCATTAATTTAATATAATCTGG
TTCCTGTTTAAATAATTCCACGATTATATTGCTAACTTCTAAGAAATGATCAATTTTTTT
GGTTTCAAGCGCCAAGTCCATTAAAGCAGCAGCATAATTATCAATAAATTTTTCACTAAT
TAACAT


>protein sequence
MLISEKFIDNYAAALMDLALETKKIDHFLEVSNIIVELFKQEPDYIKLMMNADIPKEERK
NILAKPFQKVIDPLILNALFLLIDREAFCYVRRIFKRLRKLINISYDVQYGNIYSTQPLT
KKQITTIETKLSKKFGYHIELVNKIDSSLLGGVRIKIKHEIIDGSIAGQLETMRQKAIHN
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© Fisunov Lab of Proteomics, 2016.