TB Genome Annotation Portal

Rv1307 (atpH)

• Current annotations:
  • TBCAP: (community-based annotations - see table at bottom of page)
  • TBDB: ATP synthase subunit B-delta
  • REFSEQ: F0F1 ATP synthase subunit delta
  • PATRIC: ATP synthase B' chain (EC 3.6.3.14) / ATP synthase delta chain (EC 3.6.3.14)
  • TUBERCULIST: Probable ATP synthase delta chain AtpH
  • NCBI: Probable ATP synthase delta chain AtpH
  • updated information (H37Rv4):
    • gene name: atpH
    • function:
    • reference:
• Type: Not Target
• Start: 1461843
• End: 1463183
• Operon:


• Trans-membrane region:
  
• Role: I.B.8 - ATP-proton motive force
• GO terms:
  • GO:0099132 - ATP hydrolysis coupled cation transmembrane transport (Uniprot)
  • GO:0046933 - proton-transporting ATP synthase activity, rotational mechanism (Uniprot)
  • GO:0045263 - proton-transporting ATP synthase complex, coupling factor F(o) (Uniprot)
  • GO:0045261 - proton-transporting ATP synthase complex, catalytic core F(1) (Uniprot)
  • GO:0040007 - growth (Uniprot)
  • GO:0016021 - integral component of membrane (Uniprot)
  • GO:0016020 - membrane (Uniprot)
  • GO:0015986 - ATP synthesis coupled proton transport (Uniprot)
  • GO:0015078 - proton transmembrane transporter activity (Uniprot)
  • GO:0008152 - metabolic process (Uniprot)
  • GO:0006811 - ion transport (Uniprot)
  • GO:0006754 - ATP biosynthetic process (Uniprot)
  • GO:0005886 - plasma membrane (Uniprot)
  • GO:0005618 - cell wall (Uniprot)
  • GO:0003824 - catalytic activity (Uniprot)
• Reaction(s) (based on iSM810 metabolic model):
  • 4 H[c] + ADP[c] + PI[c] <=> ATP[c]
• Gene Expression Profile (Transcriptional Responses to Drugs; Boshoff et al, 2004)
• Gene Modules extracted from cluster analysis of 249 transcriptomic datasets using ICA
• Orthologs among selected mycobacteria
• Protein structure:
• Search for Homologs in PDB
• Top 10 Homologs in PDB (as of Nov 2020):
  

  PDB	aa ident	species	PDB title
  7JGC	59%	Mycolicibacterium smegmatis	Cryo-EM structure of bedaquiline-saturated Mycobacterium smegmatis ATP synthase FO region
  7JGB	59%	Mycolicibacterium smegmatis	Cryo-EM structure of bedaquiline-free Mycobacterium smegmatis ATP synthase FO region
  7JGA	59%	Mycolicibacterium smegmatis	Cryo-EM structure of bedaquiline-saturated Mycobacterium smegmatis ATP synthase rotational state 3
  7JG9	59%	Mycolicibacterium smegmatis	Cryo-EM structure of bedaquiline-saturated mycobacterium smegmatis ATP synthase rotational state 2 (backbone model)
  7JG8	59%	Mycolicibacterium smegmatis	Cryo-EM structure of bedaquiline-saturated Mycobacterium smegmatis ATP synthase rotational state 1 (backbone model)
  7JG7	59%	Mycolicibacterium smegmatis	Cryo-EM structure of bedaquiline-free Mycobacterium smegmatis ATP synthase rotational state 3 (backbone model)
  7JG6	59%	Mycolicibacterium smegmatis	Cryo-EM structure of bedaquiline-free Mycobacterium smegmatis ATP synthase rotational state 2 (backbone model)
  7JG5	59%	Mycolicibacterium smegmatis	Cryo-EM structure of bedaquiline-free Mycobacterium smegmatis ATP synthase rotational state 1

• Links to additional information on atpH:
  • TBDB (updated)
  • Phyre2 structure prediction, model: final.casp.pdb (from Mao et al, 2013)
  • UniProt
  • AlphaFold model
  • Vulnerability = -7.703 (from Jeremy Rock's lab)
  • KEGG - nucleotide and amino acid sequences of gene
  • Mycobrowser
  • PATRIC
  • BioCyc
  • Systems Biology

Amino Acid Sequence

MSTFIGQLFGFAVIVYLVWRFIVPLVGRLMSARQDTVRQQLADAAAAADRLAEASQAHTKALEDAKSEAHRVVEEARTDAERIAEQLEAQADVEAERIKM
QGARQVDLIRAQLTRQLRLELGHESVRQARELVRNHVADQAQQSATVDRFLDQLDAMAPATADVDYPLLAKMRSASRRALTSLVDWFGTMAQDLDHQGLT
TLAGELVSVARLLDREAVVTRYLTVPAEDATPRIRLIERLVSGKVGAPTLEVLRTAVSKRWSANSDLIDAIEHVSRQALLELAERAGQVDEVEDQLFRFS
RILDVQPRLAILLGDCAVPAEGRVRLLRKVLERADSTVNPVVVALLSHTVELLRGQAVEEAVLFLAEVAVARRGEIVAQVGAAAELSDAQRTRLTEVLSR
IYGHPVTVQLHIDAALLGGLSIAVGDEVIDGTLSSRLAAAEARLPD

Additional Information