Reviewed, UniProtKB/Swiss-Prot P0ABA6 (ATPG_ECOLI)

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	287 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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: Miscellaneous discrepancy. Sequencing errors.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Cell inner membrane Cell membrane Membrane
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	ATP synthesis coupled proton transport Inferred from direct assay. Source: UniProtKB
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW proton-transporting ATP synthase complex, catalytic core F(1) Inferred from mutant phenotype. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: HAMAP protein binding Inferred from physical interaction. Source: IntAct proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
hemK	P0ACC1	1	EBI-544306,EBI-1122814

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 287

287

ATP synthase gamma chain HAMAP MF_00815

PRO_0000073282

Secondary structure

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287

Helix Strand Turn

Details...

Helix

20 – 57

38

Helix

66 – 68

3

Beta strand

74 – 81

8

Beta strand

84 – 86

3

Helix

91 – 108

18

Beta strand

112 – 119

8

Helix

120 – 129

10

Beta strand

133 – 137

5

Helix

147 – 161

15

Beta strand

168 – 177

10

Beta strand

180 – 190

11

Beta strand

207 – 210

4

Helix

212 – 247

36

Sequences

	Sequence		Length	Mass (Da)
	P0ABA6-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 2417A4B8FBDB8EF8	FASTA	287	31,577
	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

References

	« Hide 'large scale' referencesShow '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: 6395859] [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: 6272217] [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: 6277310] [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: 6301339] [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: 7686882] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 7508444] [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: 2138624] [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: 16079137] [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: 10570135] [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.

PIR

PWECG. A01038.

RefSeq

AP_004054.1.
NP_418189.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D8S	X-ray	4.40	G	1-287	[»]
1FS0	X-ray	2.10	G	19-248	[»]

SMR

P0ABA6. Positions 3-268.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0ABA6. 10 interactions.

STRING

P0ABA6.

Protein family/group databases

TCDB

3.A.2.1.1. H+- or Na+-translocating F-type, V-type and A-type ATPase (F-ATPase) superfamily.

Genome annotation databases

GeneID

948243.

GenomeReviews

Gene locus JW3711 in contig AP009048_GR.
Gene locus b3733 in contig U00096_GR.

KEGG

ecj:JW3711.
eco:b3733.

Organism-specific databases

EchoBASE

EB0102.

EcoGene

EG10104. atpG.

CMR

Search...

Phylogenomic databases

eggNOG

COG0224.

HOGENOM

HBG586593.

OMA

NNASDNA.

Enzyme and pathway databases

BioCyc

EcoCyc:ATPG-MONOMER.
ECOL168927:B3733-MONOMER.
MetaCyc:ATPG-MONOMER.

Gene expression databases

Genevestigator

P0ABA6.

Family and domain databases

HAMAP

MF_00815. ATP_synth_gamma_bact.
[Tree]

InterPro

IPR000131. ATPase_F1-cplx_gsu.
[Graphical view]

PANTHER

PTHR11693. ATPase_F1_gamma. 1 hit.

Pfam

PF00231. ATP-synt. 1 hit.
[Graphical view]

PRINTS

PR00126. ATPASEGAMMA.

TIGRFAMs

TIGR01146. ATPsyn_F1gamma. 1 hit.

PROSITE

PS00153. ATPASE_GAMMA. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ATPG_ECOLI

Accession

Primary (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:	February 9, 2010
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)