RegulonDB RegulonDB 10.9: Gene Form
   

atpB gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

atpB atpI atpE TSS_4344 TSS_4344 atpBp1 atpBp1 atpBp2 atpBp2 TSS_4343 TSS_4343 TSS_4342 (cluster) TSS_4342 (cluster) TSS_4341 (cluster) TSS_4341 (cluster) TSS_4340 (cluster) TSS_4340 (cluster) TSS_4339 (cluster) TSS_4339 (cluster) TSS_4338 (cluster) TSS_4338 (cluster) TSS_4337 (cluster) TSS_4337 (cluster) TSS_4336 TSS_4336 TSS_4335 TSS_4335 TSS_4334 TSS_4334 TSS_4333 TSS_4333 TSS_4332 (cluster) TSS_4332 (cluster) TSS_4331 TSS_4331 TSS_4330 (cluster) TSS_4330 (cluster) TSS_4329 TSS_4329 TSS_4328 TSS_4328

Gene      
Name: atpB    Texpresso search in the literature
Synonym(s): ECK3731, EG10099, b3738, papD, uncB
Genome position(nucleotides): 3921236 <-- 3922051 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
50.25
External database links:  
ASAP:
ABE-0012222
CGSC:
32
ECHOBASE:
EB0097
ECOLIHUB:
atpB
OU-MICROARRAY:
b3738
STRING:
511145.b3738
COLOMBOS: atpB


Product      
Name: ATP synthase Fo complex subunit a
Synonym(s): ATP synthase Fo complex - a subunit, AtpB, PapD, UncB, chain A, protein 6
Sequence: Get amino acid sequence Fasta Format
Cellular location: inner membrane
Molecular weight: 30.303
Isoelectric point: 6.898
Motif(s):
 
Type Positions Sequence
220 -> 240 LIFILIAGLLPWWSQWILNVP
179 -> 182 TLQP
206 -> 206 S
214 -> 214 N
207 -> 207 L

 

Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.3 - energy metabolism, carbon --> 1.3.8 - ATP proton motive force interconversion
  2 - information transfer --> 2.3 - protein related --> 2.3.4 - chaperoning, repair (refolding)
  4 - transport --> 4.3 - Primary Active Transporters --> 4.3.A - Pyrophosphate Bond (ATP; GTP; P2) Hydrolysis-driven Active Transporters --> 4.3.A.2 - The H+- or Na+-translocating F-type, V-type and A-type ATPase (F-ATPase) Su
  6 - cell structure --> 6.1 - membrane
Gene Ontology Terms (GO)  
cellular_component GO:0016020 - membrane
GO:0005886 - plasma membrane
GO:0005887 - integral component of plasma membrane
GO:0016021 - integral component of membrane
GO:0045263 - proton-transporting ATP synthase complex, coupling factor F(o)
molecular_function GO:0015078 - proton transmembrane transporter activity
GO:0046933 - proton-transporting ATP synthase activity, rotational mechanism
biological_process GO:0006754 - ATP biosynthetic process
GO:0006811 - ion transport
GO:0015986 - ATP synthesis coupled proton transport
GO:0042777 - plasma membrane ATP synthesis coupled proton transport
Note(s): Note(s): ...[more].
Reference(s): [1] Aksimentiev A., et al., 2004
[2] Angevine CM., et al., 2007
[3] Cain BD., et al., 1989
[4] Cain BD., et al., 1988
[5] DeLeon-Rangel J., et al., 2003
[6] Dong H., et al., 2010
[7] Duser MG., et al., 2008
[8] Hartzog PE., et al., 1993
[9] Jindal S., et al., 2019
[10] Lightowlers RN., et al., 1987
[11] Long JC., et al., 2002
[12] Moore KJ., et al., 2013
[13] Paule CR., et al., 1989
[14] Steed PR., et al., 2014
[15] Vik SB., et al., 1994
[16] Vik SB., et al., 1990
[17] Vik SB., et al., 1998
[18] Zhang D., et al., 2003
[19] Zhang D., et al., 2003
External database links:  
DIP:
DIP-47956N
ECOCYC:
ATPB-MONOMER
ECOLIWIKI:
b3738
INTERPRO:
IPR035908
INTERPRO:
IPR023011
INTERPRO:
IPR000568
MINT:
P0AB98
MODBASE:
P0AB98
PDB:
1C17
PDB:
5T4Q
PDB:
5T4P
PDB:
5T4O
PFAM:
PF00119
PRIDE:
P0AB98
PRINTS:
PR00123
PRODB:
PRO_000022187
PROSITE:
PS00449
REFSEQ:
NP_418194
SMR:
P0AB98
UNIPROT:
P0AB98


Operon      
Name: atpIBEFHAGDC         
Operon arrangement:
Transcription unit        Promoter
atpBEFHAGDC
atpBEFHAGDC
atpIBEFHAGDC


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter TSS_4328 3920997 reverse nd [RS-EPT-CBR] [20]
  promoter TSS_4329 3921003 reverse nd [RS-EPT-CBR] [20]
  promoter TSS_4330 (cluster) 3921379 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [20]
  promoter TSS_4331 3921382 reverse nd [RS-EPT-CBR] [20]
  promoter TSS_4332 (cluster) 3921385 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [20]
  promoter TSS_4333 3921390 reverse nd [RS-EPT-CBR] [20]
  promoter TSS_4334 3921401 reverse nd [RS-EPT-CBR] [20]
  promoter TSS_4335 3921709 reverse nd [RS-EPT-CBR] [20]
  promoter TSS_4336 3921775 reverse nd [RS-EPT-CBR] [20]
  promoter TSS_4337 (cluster) 3921812 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [20]
  promoter TSS_4338 (cluster) 3921818 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [20]
  promoter TSS_4339 (cluster) 3921823 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [20]
  promoter TSS_4340 (cluster) 3921829 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [20]
  promoter TSS_4341 (cluster) 3922078 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [20]
  promoter TSS_4342 (cluster) 3922116 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [20]
  promoter TSS_4343 3922124 reverse nd [RS-EPT-CBR] [20]
  promoter TSS_4344 3922273 reverse nd [RS-EPT-CBR] [20]


Evidence    

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates



Reference(s)    

 [1] Aksimentiev A., Balabin IA., Fillingame RH., Schulten K., 2004, Insights into the molecular mechanism of rotation in the Fo sector of ATP synthase., Biophys J 86(3):1332-44

 [2] Angevine CM., Herold KA., Vincent OD., Fillingame RH., 2007, Aqueous access pathways in ATP synthase subunit a. Reactivity of cysteine substituted into transmembrane helices 1, 3, and 5., J Biol Chem 282(12):9001-7

 [3] Cain BD., Simoni RD., 1989, Proton translocation by the F1F0ATPase of Escherichia coli. Mutagenic analysis of the a subunit., J Biol Chem 264(6):3292-300

 [4] Cain BD., Simoni RD., 1988, Interaction between Glu-219 and His-245 within the a subunit of F1F0-ATPase in Escherichia coli., J Biol Chem 263(14):6606-12

 [5] DeLeon-Rangel J., Zhang D., Vik SB., 2003, The role of transmembrane span 2 in the structure and function of subunit a of the ATP synthase from Escherichia coli., Arch Biochem Biophys 418(1):55-62

 [6] Dong H., Fillingame RH., 2010, Chemical reactivities of cysteine substitutions in subunit a of ATP synthase define residues gating H+ transport from each side of the membrane., J Biol Chem 285(51):39811-8

 [7] Duser MG., Bi Y., Zarrabi N., Dunn SD., Borsch M., 2008, The proton-translocating a subunit of F0F1-ATP synthase is allocated asymmetrically to the peripheral stalk., J Biol Chem 283(48):33602-10

 [8] Hartzog PE., Cain BD., 1993, Mutagenic analysis of the a subunit of the F1F0 ATP synthase in Escherichia coli: Gln-252 through Tyr-263., J Bacteriol 175(5):1337-43

 [9] Jindal S., Yang L., Day PJ., Kell DB., 2019, Involvement of multiple influx and efflux transporters in the accumulation of cationic fluorescent dyes by Escherichia coli., BMC Microbiol 19(1):195

 [10] Lightowlers RN., Howitt SM., Hatch L., Gibson F., Cox GB., 1987, The proton pore in the Escherichia coli F0F1-ATPase: a requirement for arginine at position 210 of the a-subunit., Biochim Biophys Acta 894(3):399-406

 [11] Long JC., DeLeon-Rangel J., Vik SB., 2002, Characterization of the first cytoplasmic loop of subunit a of the Escherichia coli ATP synthase by surface labeling, cross-linking, and mutagenesis., J Biol Chem 277(30):27288-93

 [12] Moore KJ., Fillingame RH., 2013, Obstruction of transmembrane helical movements in subunit a blocks proton pumping by F1Fo ATP synthase., J Biol Chem 288(35):25535-41

 [13] Paule CR., Fillingame RH., 1989, Mutations in three of the putative transmembrane helices of subunit a of the Escherichia coli F1F0-ATPase disrupt ATP-driven proton translocation., Arch Biochem Biophys 274(1):270-84

 [14] Steed PR., Kraft KA., Fillingame RH., 2014, Interacting cytoplasmic loops of subunits a and c of Escherichia coli F1F0 ATP synthase gate H+ transport to the cytoplasm., Proc Natl Acad Sci U S A 111(47):16730-5

 [15] Vik SB., Antonio BJ., 1994, A mechanism of proton translocation by F1F0 ATP synthases suggested by double mutants of the a subunit., J Biol Chem 269(48):30364-9

 [16] Vik SB., Lee D., Curtis CE., Nguyen LT., 1990, Mutagenesis of the a subunit of the F1F0-ATP synthase from Escherichia coli in the region of Asn-192., Arch Biochem Biophys 282(1):125-31

 [17] Vik SB., Patterson AR., Antonio BJ., 1998, Insertion scanning mutagenesis of subunit a of the F1F0 ATP synthase near His245 and implications on gating of the proton channel., J Biol Chem 273(26):16229-34

 [18] Zhang D., Vik SB., 2003, Helix packing in subunit a of the Escherichia coli ATP synthase as determined by chemical labeling and proteolysis of the cysteine-substituted protein., Biochemistry 42(2):331-7

 [19] Zhang D., Vik SB., 2003, Close proximity of a cytoplasmic loop of subunit a with c subunits of the ATP synthase from Escherichia coli., J Biol Chem 278(14):12319-24

 [20] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.


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