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P0ABA6 (ATPG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase gamma chain
Alternative name(s):
ATP synthase F1 sector gamma subunit
F-ATPase gamma subunit
Gene names
Name:atpG
Synonyms:papC, uncG
Ordered Locus Names:b3733, JW3711
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length287 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF0 complex. HAMAP-Rule MF_00815

Subunit structure

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c. Ref.10

Subcellular location

Cell inner membrane; Peripheral membrane protein Ref.10.

Sequence similarities

Belongs to the ATPase gamma chain family.

Sequence caution

The sequence CAA23597.1 differs from that shown. Reason: Frameshift at several positions.

The sequence CAA23597.1 differs from that shown. Reason: Sequencing errors.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

atpCP0A6E63EBI-544306,EBI-544362

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 287287ATP synthase gamma chain HAMAP-Rule MF_00815
PRO_0000073282

Secondary structure

.............................. 287
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0ABA6 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 2417A4B8FBDB8EF8

FASTA28731,577
        10         20         30         40         50         60 
MAGAKEIRSK IASVQNTQKI TKAMEMVAAS KMRKSQDRMA ASRPYAETMR KVIGHLAHGN 

        70         80         90        100        110        120 
LEYKHPYLED RDVKRVGYLV VSTDRGLCGG LNINLFKKLL AEMKTWTDKG VQCDLAMIGS 

       130        140        150        160        170        180 
KGVSFFNSVG GNVVAQVTGM GDNPSLSELI GPVKVMLQAY DEGRLDKLYI VSNKFINTMS 

       190        200        210        220        230        240 
QVPTISQLLP LPASDDDDLK HKSWDYLYEP DPKALLDTLL RRYVESQVYQ GVVENLASEQ 

       250        260        270        280 
AARMVAMKAA TDNGGSLIKE LQLVYNKARQ ASITQELTEI VSGAAAV 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequence around the Escherichia coli unc operon. Completion of the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and phoS."
Walker J.E., Gay N.J., Saraste M., Eberle A.N.
Biochem. J. 224:799-815(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The atp operon: nucleotide sequence of the genes for the gamma, beta, and epsilon subunits of Escherichia coli ATP synthase."
Saraste M., Gay N.J., Eberle A., Runswick M.J., Walker J.E.
Nucleic Acids Res. 9:5287-5296(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Nucleotide sequence of the genes coding for alpha, beta and gamma subunits of the proton-translocating ATPase of Escherichia coli."
Kanazawa H., Kayano T., Mabuchi K., Futai M.
Biochem. Biophys. Res. Commun. 103:604-612(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Structure and function of H+-ATPase: what we have learned from Escherichia coli H+-ATPase."
Kanazawa H., Futai M.
Ann. N. Y. Acad. Sci. 402:45-64(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[7]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]"Structure of the gamma subunit of Escherichia coli F1 ATPase probed in trypsin digestion and biotin-avidin binding studies."
Tang C., Wilkens S., Capaldi R.A.
J. Biol. Chem. 269:4467-4472(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-9; 72-81; 203-208 AND 214-220.
[9]"H(+)-ATPase gamma subunit of Escherichia coli. Role of the conserved carboxyl-terminal region."
Iwamoto A., Miki J., Maeda M., Futai M.
J. Biol. Chem. 265:5043-5048(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 261-287.
[10]"Protein complexes of the Escherichia coli cell envelope."
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION.
Strain: BL21-DE3.
[11]"Structural features of the gamma subunit of the Escherichia coli F(1) ATPase revealed by a 4.4-A resolution map obtained by X-ray crystallography."
Hausrath A.C., Grueber G., Matthews B.W., Capaldi R.A.
Proc. Natl. Acad. Sci. U.S.A. 96:13697-13702(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.4 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X01631 Genomic DNA. Translation: CAA25781.1.
V00267 Genomic DNA. Translation: CAA23526.1.
J01594 Genomic DNA. Translation: AAA24736.1. Frameshift.
V00312 Genomic DNA. Translation: CAA23597.1. Sequence problems.
M25464 Genomic DNA. Translation: AAA83874.1.
L10328 Genomic DNA. Translation: AAA62085.1.
U00096 Genomic DNA. Translation: AAC76756.1.
AP009048 Genomic DNA. Translation: BAE77555.1.
M34095 Genomic DNA. Translation: AAA24742.1.
PIRPWECG. A01038.
RefSeqNP_418189.1. NC_000913.3.
YP_491696.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8SX-ray4.40G1-287[»]
1FS0X-ray2.10G19-248[»]
3OAAX-ray3.26G/O/W/e2-287[»]
ProteinModelPortalP0ABA6.
SMRP0ABA6. Positions 2-285.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35938N.
IntActP0ABA6. 15 interactions.
STRING511145.b3733.

Protein family/group databases

TCDB3.A.2.1.1. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Proteomic databases

PaxDbP0ABA6.
PRIDEP0ABA6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76756; AAC76756; b3733.
BAE77555; BAE77555; BAE77555.
GeneID12934007.
948243.
KEGGecj:Y75_p3435.
eco:b3733.
PATRIC32122963. VBIEscCol129921_3857.

Organism-specific databases

EchoBASEEB0102.
EcoGeneEG10104. atpG.

Phylogenomic databases

eggNOGCOG0224.
HOGENOMHOG000215912.
KOK02115.
OMADRGMCGG.
OrthoDBEOG6R5C97.
PhylomeDBP0ABA6.
ProtClustDBPRK05621.

Enzyme and pathway databases

BioCycEcoCyc:ATPG-MONOMER.
ECOL316407:JW3711-MONOMER.
MetaCyc:ATPG-MONOMER.

Gene expression databases

GenevestigatorP0ABA6.

Family and domain databases

HAMAPMF_00815. ATP_synth_gamma_bact.
InterProIPR000131. ATPase_F1-cplx_gsu.
IPR023632. ATPase_F1_gsu_CS.
IPR023633. ATPase_F1_gsu_dom.
[Graphical view]
PANTHERPTHR11693. PTHR11693. 1 hit.
PfamPF00231. ATP-synt. 1 hit.
[Graphical view]
PRINTSPR00126. ATPASEGAMMA.
SUPFAMSSF52943. SSF52943. 1 hit.
TIGRFAMsTIGR01146. ATPsyn_F1gamma. 1 hit.
PROSITEPS00153. ATPASE_GAMMA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0ABA6.
PROP0ABA6.

Entry information

Entry nameATPG_ECOLI
AccessionPrimary (citable) accession number: P0ABA6
Secondary accession number(s): P00837, P00838, Q2M851
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene