Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0ABA6

- ATPG_ECOLI

UniProt

P0ABA6 - ATPG_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

ATP synthase gamma chain

Gene

atpG

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. proton-transporting ATPase activity, rotational mechanism Source: EcoCyc
  3. proton-transporting ATP synthase activity, rotational mechanism Source: EcoCyc

GO - Biological processi

  1. plasma membrane ATP synthesis coupled proton transport Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

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

Protein family/group databases

TCDBi3.A.2.1.1. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase gamma chain
Alternative name(s):
ATP synthase F1 sector gamma subunit
F-ATPase gamma subunit
Gene namesi
Name:atpG
Synonyms:papC, uncG
Ordered Locus Names:b3733, JW3711
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10104. atpG.

Subcellular locationi

Cell inner membrane 1 Publication; Peripheral membrane protein 1 Publication

GO - Cellular componenti

  1. membrane Source: UniProtKB
  2. plasma membrane Source: UniProtKB-HAMAP
  3. proton-transporting ATP synthase complex, catalytic core F(1) Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, CF(1), Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 287287ATP synthase gamma chainPRO_0000073282Add
BLAST

Proteomic databases

PaxDbiP0ABA6.
PRIDEiP0ABA6.

Expressioni

Gene expression databases

GenevestigatoriP0ABA6.

Interactioni

Subunit structurei

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
atpCP0A6E64EBI-544306,EBI-544362

Protein-protein interaction databases

DIPiDIP-35938N.
IntActiP0ABA6. 15 interactions.
STRINGi511145.b3733.

Structurei

Secondary structure

1
287
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 5738
Turni61 – 633
Helixi66 – 683
Beta strandi74 – 818
Beta strandi84 – 863
Helixi91 – 10818
Beta strandi112 – 1198
Helixi120 – 12910
Beta strandi133 – 1375
Helixi147 – 16115
Beta strandi168 – 17710
Beta strandi180 – 19011
Turni196 – 1983
Beta strandi207 – 2104
Helixi212 – 24736

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8SX-ray4.40G1-287[»]
1FS0X-ray2.10G19-248[»]
3OAAX-ray3.26G/O/W/e2-287[»]
ProteinModelPortaliP0ABA6.
SMRiP0ABA6. Positions 2-285.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABA6.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase gamma chain family.Curated

Phylogenomic databases

eggNOGiCOG0224.
HOGENOMiHOG000215912.
InParanoidiP0ABA6.
KOiK02115.
OMAiASIGYKH.
OrthoDBiEOG6R5C97.
PhylomeDBiP0ABA6.

Family and domain databases

HAMAPiMF_00815. ATP_synth_gamma_bact.
InterProiIPR000131. ATPase_F1-cplx_gsu.
IPR023632. ATPase_F1_gsu_CS.
IPR023633. ATPase_F1_gsu_dom.
[Graphical view]
PANTHERiPTHR11693. PTHR11693. 1 hit.
PfamiPF00231. ATP-synt. 1 hit.
[Graphical view]
PRINTSiPR00126. ATPASEGAMMA.
SUPFAMiSSF52943. SSF52943. 1 hit.
TIGRFAMsiTIGR01146. ATPsyn_F1gamma. 1 hit.
PROSITEiPS00153. ATPASE_GAMMA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ABA6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGAKEIRSK IASVQNTQKI TKAMEMVAAS KMRKSQDRMA ASRPYAETMR
60 70 80 90 100
KVIGHLAHGN LEYKHPYLED RDVKRVGYLV VSTDRGLCGG LNINLFKKLL
110 120 130 140 150
AEMKTWTDKG VQCDLAMIGS KGVSFFNSVG GNVVAQVTGM GDNPSLSELI
160 170 180 190 200
GPVKVMLQAY DEGRLDKLYI VSNKFINTMS QVPTISQLLP LPASDDDDLK
210 220 230 240 250
HKSWDYLYEP DPKALLDTLL RRYVESQVYQ GVVENLASEQ AARMVAMKAA
260 270 280
TDNGGSLIKE LQLVYNKARQ ASITQELTEI VSGAAAV
Length:287
Mass (Da):31,577
Last modified:July 21, 1986 - v1
Checksum:i2417A4B8FBDB8EF8
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA01038. PWECG.
RefSeqiNP_418189.1. NC_000913.3.
YP_491696.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76756; AAC76756; b3733.
BAE77555; BAE77555; BAE77555.
GeneIDi12934007.
948243.
KEGGiecj:Y75_p3435.
eco:b3733.
PATRICi32122963. VBIEscCol129921_3857.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A01038. PWECG.
RefSeqi NP_418189.1. NC_000913.3.
YP_491696.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D8S X-ray 4.40 G 1-287 [» ]
1FS0 X-ray 2.10 G 19-248 [» ]
3OAA X-ray 3.26 G/O/W/e 2-287 [» ]
ProteinModelPortali P0ABA6.
SMRi P0ABA6. Positions 2-285.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35938N.
IntActi P0ABA6. 15 interactions.
STRINGi 511145.b3733.

Protein family/group databases

TCDBi 3.A.2.1.1. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Proteomic databases

PaxDbi P0ABA6.
PRIDEi P0ABA6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76756 ; AAC76756 ; b3733 .
BAE77555 ; BAE77555 ; BAE77555 .
GeneIDi 12934007.
948243.
KEGGi ecj:Y75_p3435.
eco:b3733.
PATRICi 32122963. VBIEscCol129921_3857.

Organism-specific databases

EchoBASEi EB0102.
EcoGenei EG10104. atpG.

Phylogenomic databases

eggNOGi COG0224.
HOGENOMi HOG000215912.
InParanoidi P0ABA6.
KOi K02115.
OMAi ASIGYKH.
OrthoDBi EOG6R5C97.
PhylomeDBi P0ABA6.

Enzyme and pathway databases

BioCyci EcoCyc:ATPG-MONOMER.
ECOL316407:JW3711-MONOMER.
MetaCyc:ATPG-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0ABA6.
PROi P0ABA6.

Gene expression databases

Genevestigatori P0ABA6.

Family and domain databases

HAMAPi MF_00815. ATP_synth_gamma_bact.
InterProi IPR000131. ATPase_F1-cplx_gsu.
IPR023632. ATPase_F1_gsu_CS.
IPR023633. ATPase_F1_gsu_dom.
[Graphical view ]
PANTHERi PTHR11693. PTHR11693. 1 hit.
Pfami PF00231. ATP-synt. 1 hit.
[Graphical view ]
PRINTSi PR00126. ATPASEGAMMA.
SUPFAMi SSF52943. SSF52943. 1 hit.
TIGRFAMsi TIGR01146. ATPsyn_F1gamma. 1 hit.
PROSITEi PS00153. ATPASE_GAMMA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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).

Entry informationi

Entry nameiATPG_ECOLI
AccessioniPrimary (citable) accession number: P0ABA6
Secondary accession number(s): P00837, P00838, Q2M851
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3