Reviewed, UniProtKB/Swiss-Prot P0ABA0 (ATPF_ECOLI)

Names and origin

Protein names

Recommended name:
    ATP synthase subunit b
Alternative name(s):
    ATP synthase F(0) sector subunit b
    F-type ATPase subunit b
      Short name=F-ATPase subunit b
    ATPase subunit I

Gene names

Name:	atpF
Synonyms:	papF, uncF
Ordered Locus Names:	b3736, JW3714

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	156 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	F1F0 ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F1 containing the extramembraneous catalytic core and F0 containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation By similarity. HAMAP MF_01398 Component of the F0 channel, it forms part of the peripheral stalk, linking F1 to F0 By similarity. HAMAP MF_01398
Subunit structure	F-type ATPases have 2 components, F1 - the catalytic core - and F0 - the membrane proton channel. F1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. F0 has three main subunits: a1, b2 and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F1 is attached to F0 by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains By similarity. Ref.12
Subcellular location	Cell inner membrane; Single-pass membrane protein By similarity Ref.12.
Sequence similarities	Belongs to the ATPase B chain family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(0) Cell inner membrane Cell membrane Membrane
Domain	Transmembrane
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	ATP synthesis coupled proton transport Inferred from mutant phenotype. Source: UniProtKB
Cellular component	anchored to membrane Inferred from direct assay. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW proton-transporting ATP synthase complex, coupling factor F(o) Inferred from mutant phenotype. Source: UniProtKB
Molecular function	hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 156

156

ATP synthase subunit b HAMAP MF_01398

PRO_0000082371

Regions

Transmembrane

11 – 31

21

Potential

Sites

Site

9

1

Mutation prevents the formation of a functional proton pore, but has a small effect on the binding of F(1) to F(0) HAMAP MF_01398

Site

131

1

Required for proton pore formation, as well as F(1) to F(0) binding HAMAP MF_01398

Experimental info

Sequence conflict

33

1

I → F in CAA23592. Ref.3

Sequence conflict

62

1

T → N in AAA24741. Ref.7

Sequence conflict

72

1

A → D in CAA23592. Ref.3

Secondary structure

1

.

.

.

.

.

156

Helix Strand Turn

Details...

Helix

4 – 24

21

Helix

63 – 120

58

Sequences

	Sequence		Length	Mass (Da)
	P0ABA0-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 51A93C8BEE9AD9DF	FASTA	156	17,264
	10 20 30 40 50 60 MNLNATILGQ AIAFVLFVLF CMKYVWPPLM AAIEKRQKEI ADGLASAERA HKDLDLAKAS 70 80 90 100 110 120 ATDQLKKAKA EAQVIIEQAN KRRSQILDEA KAEAEQERTK IVAQAQAEIE AERKRAREEL 130 140 150 RKQVAILAVA GAEKIIERSV DEAANSDIVD KLVAEL

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 promoter and the genes for the membrane proteins, and the delta subunit of Escherichia coli ATP-synthase." Gay N.J., Walker J.E. Nucleic Acids Res. 9:3919-3926(1981) [PubMed: 6272190] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Nucleotide sequence of the genes for F0 components of the proton-translocating ATPase from Escherichia coli: prediction of the primary structure of F0 subunits." Kanazawa H., Mabuchi K., Kayano T., Noumi T., Sekiya T., Futai M. Biochem. Biophys. Res. Commun. 103:613-620(1981) [PubMed: 6277311] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The nucleotide sequence of the atp genes coding for the F0 subunits a, b, c and the F1 subunit delta of the membrane bound ATP synthase of Escherichia coli." Nielsen J., Hansen F.G., Hoppe J., Friedl P., von Meyenburg K. Mol. Gen. Genet. 184:33-39(1981) [PubMed: 6278247] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"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].
[6]	"Role of the b subunit of the Escherichia coli proton-translocating ATPase. A mutagenic analysis." Porter A.C.G., Kumamoto C., Aldape K., Simoni R.D. J. Biol. Chem. 260:8182-8187(1985) [PubMed: 2861200] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"Nucleotide sequence of the gene coding for the delta subunit of proton translocating ATPase of Escherichia coli." Mabuchi K., Kanazawa H., Kayano T., Futai M. Biochem. Biophys. Res. Commun. 102:172-179(1981) [PubMed: 6458296] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 132-156.
[11]	"Targeted mutagenesis of the b subunit of F1F0 ATP synthase in Escherichia coli: Glu-77 through Gln-85." McCormick K.A., Cain B.D. J. Bacteriol. 173:7240-7248(1991) [PubMed: 1682301] [Abstract] Cited for: MUTAGENESIS OF REGION 77-GLU--GLN-85.
[12]	"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.
[13]	"Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthase." Dmitriev O., Jones P.C., Jiang W., Fillingame R.H. J. Biol. Chem. 274:15598-15604(1999) [PubMed: 10336456] [Abstract] Cited for: STRUCTURE BY NMR OF 1-34.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J01594 Genomic DNA. Translation: AAA24733.1.
X01631 Genomic DNA. Translation: CAA25778.1.
V00264 Genomic DNA. Translation: CAA23516.1.
V00310 Genomic DNA. Translation: CAA23592.1.
V00266 Genomic DNA. Translation: CAA23523.1.
M25464 Genomic DNA. Translation: AAA83871.1.
M10422 Genomic DNA. Translation: AAA24741.1.
L10328 Genomic DNA. Translation: AAA62088.1.
U00096 Genomic DNA. Translation: AAC76759.1.
AP009048 Genomic DNA. Translation: BAE77552.1.
M12212 Unassigned DNA. Translation: AAA20043.1.

PIR

LWECB. D93732.

RefSeq

AP_004051.1.
NP_418192.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B9U	NMR	-	A	1-34	[»]
1L2P	X-ray	1.55	A	62-122	[»]
2KHK	NMR	-	A	30-82	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P0ABA0.

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.

2-D gel databases

SWISS-2DPAGE

P0ABA0.

Genome annotation databases

GeneID

948247.

GenomeReviews

Gene locus JW3714 in contig AP009048_GR.
Gene locus b3736 in contig U00096_GR.

KEGG

ecj:JW3714.
eco:b3736.

Organism-specific databases

EchoBASE

EB0101.

EcoGene

EG10103. atpF.

CMR

Search...

Phylogenomic databases

eggNOG

COG0711.

HOGENOM

HBG617328.

OMA

KRSGTID.

Enzyme and pathway databases

BioCyc

EcoCyc:ATPF-MONOMER.
ECOL168927:B3736-MONOMER.
MetaCyc:ATPF-MONOMER.

Gene expression databases

Genevestigator

P0ABA0.

Family and domain databases

HAMAP

MF_01398. ATP_synth_b_bact.
[Tree]

InterPro

IPR002146. ATPase_F0-cplx_b/b'su_bac.
IPR005864. ATPase_F0-cplx_bsu_bac.
[Graphical view]

Pfam

PF00430. ATP-synt_B. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01144. ATP_synt_b. 1 hit.

ProtoNet

Search...

Entry information

Entry name

ATPF_ECOLI

Accession

Primary (citable) accession number: P0ABA0
Secondary accession number(s): P00859, Q2M854

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	February 9, 2010
This is version 49 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)