atpF

Functionⁱ

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.UniRule annotation

Component of the F₀ channel, it forms part of the peripheral stalk, linking F₁ to F₀.UniRule annotation

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	9	Mutation prevents the formation of a functional proton pore, but has a small effect on the binding of F(1) to F(0)		1
Siteⁱ	131	Required for proton pore formation, as well as F(1) to F(0) binding		1

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

ATP synthesis coupled proton transport Source: InterPro

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Biological process

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCycⁱ	EcoCyc:ATPF-MONOMER MetaCyc:ATPF-MONOMER

BioCycⁱ

EcoCyc:ATPF-MONOMER
MetaCyc:ATPF-MONOMER

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

TCDBⁱ

3.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 subunit bUniRule annotation Alternative name(s): ATP synthase F(0) sector subunit bUniRule annotation ATPase subunit IUniRule annotation F-type ATPase subunit bUniRule annotation Short name: F-ATPase subunit bUniRule annotation
Gene namesⁱ	Name:atpFUniRule annotation Synonyms:papF, uncF Ordered Locus Names:b3736, JW3714
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG10103 atpF

EcoGeneⁱ

EG10103 atpF

Subcellular locationⁱ

Cell inner membrane
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_01398
; Single-pass membrane protein
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_01398

Topology

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transmembraneⁱ	11 – 31	HelicalUniRule annotationAdd BLAST		21

GO - Cellular componentⁱ

anchored component of membrane
Source: EcoliWiki
Inferred from direct assayⁱ
- 2863271
integral component of membrane Source: UniProtKB-KW
plasma membrane Source: UniProtKB-SubCell
proton-transporting ATP synthase complex, coupling factor F(o)
Source: EcoliWiki
Inferred from mutant phenotypeⁱ
- 6460031

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell inner membrane, Cell membrane, CF(0), Membrane

Pathology & Biotechⁱ

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB03091 4-Amido-4-Carbamoyl-Butyric Acid

DrugBankⁱ

DB03091 4-Amido-4-Carbamoyl-Butyric Acid

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000082371	1 – 156	ATP synthase subunit bAdd BLAST		156

Proteomic databases

EPDⁱ	P0ABA0
PaxDbⁱ	P0ABA0
PRIDEⁱ	P0ABA0

2D gel databases

SWISS-2DPAGEⁱ	P0ABA0

SWISS-2DPAGEⁱ

P0ABA0

Interactionⁱ

Subunit structureⁱ

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.UniRule annotation

Protein-protein interaction databases

BioGridⁱ	4262109, 80 interactors
Database of interacting proteins More...DIPⁱ	DIP-35994N
IntActⁱ	P0ABA0, 2 interactors
STRINGⁱ	316385.ECDH10B_3923

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	4 – 24	Combined sources	21
Helixⁱ	26 – 33	Combined sources	8
Helixⁱ	63 – 120	Combined sources	58

3D structure databases

ProteinModelPortalⁱ	P0ABA0
SMRⁱ	P0ABA0
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P0ABA0

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the ATPase B chain family.UniRule annotation

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	ENOG4107Z6K Bacteria COG0711 LUCA
HOGENOMⁱ	HOG000015378
InParanoidⁱ	P0ABA0
KEGG Orthology (KO) More...KOⁱ	K02109
OMAⁱ	KFAWKPI
PhylomeDBⁱ	P0ABA0

Family and domain databases

HAMAPⁱ	MF_01398 ATP_synth_b_bprime, 1 hit
InterProⁱ	View protein in InterPro IPR028987 ATP_synth_B-like_membr_sf IPR002146 ATP_synth_b/b'su_bac/chlpt IPR005864 ATP_synth_F0_bsu_bac
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00430 ATP-synt_B, 1 hit
SUPFAMⁱ	SSF81573 SSF81573, 1 hit
TIGRFAMsⁱ	TIGR01144 ATP_synt_b, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P0ABA0-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MNLNATILGQ AIAFVLFVLF CMKYVWPPLM AAIEKRQKEI ADGLASAERA 
        60         70         80         90        100
HKDLDLAKAS ATDQLKKAKA EAQVIIEQAN KRRSQILDEA KAEAEQERTK 
       110        120        130        140        150
IVAQAQAEIE AERKRAREEL RKQVAILAVA GAEKIIERSV DEAANSDIVD 

KLVAEL

Length:156

Mass (Da):17,264

Last modified:July 21, 1986 - v1

Checksum:ⁱ51A93C8BEE9AD9DF

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	33	I → F in CAA23592 (PubMed:6277311).Curated	1
Sequence conflictⁱ	62	T → N in AAA24741 (PubMed:7686882).Curated	1
Sequence conflictⁱ	72	A → D in CAA23592 (PubMed:6277311).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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
PIRⁱ	D93732 LWECB
NCBI Reference Sequences More...RefSeqⁱ	NP_418192.1, NC_000913.3 WP_001052219.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC76759; AAC76759; b3736 BAE77552; BAE77552; BAE77552
GeneIDⁱ	948247
KEGGⁱ	ecj:JW3714 eco:b3736
PATRICⁱ	fig\|1411691.4.peg.2964

Protein	Similar proteins		Species	Score	Length
P0ABA0	ATP synthase subunit b		ECO24		156
ATP synthase subunit b		ECO57		156
ATP synthase subunit b		ECO5E		156
ATP synthase subunit b		ECODH		156
ATP synthase subunit b		ECOHS		156
+200

Protein	Similar proteins		Species	Score	Length
P0ABA0	ATP synthase subunit b		PECAS		156
ATP synthase subunit b		PECCA		156
ATP synthase subunit b		Pectobacterium carotovorum subsp. brasiliense		156
ATP synthase subunit b		Pectobacterium polaris		156
ATP synthase subunit b		Pectobacterium carotovorum subsp. actinidiae		156
+704

Protein	Similar proteins		Species	Score	Length
P0ABA0	ATP synthase subunit b		PSEMY		156
ATP synthase subunit b		PSEME		156
ATP synthase subunit b		Pseudomonas sp. 63_8		156
ATP synthase subunit b		PSEOL		156
ATP synthase subunit b		Pseudomonas oleovorans subsp. oleovorans		156
+2703

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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
PIRⁱ	D93732 LWECB
NCBI Reference Sequences More...RefSeqⁱ	NP_418192.1, NC_000913.3 WP_001052219.1, NZ_LN832404.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	[»]
	5T4O	electron microscopy	6.90	I/J	2-156	[»]
	5T4P	electron microscopy	7.77	I/J	2-156	[»]
	5T4Q	electron microscopy	8.53	I/J	2-156	[»]
ProteinModelPortalⁱ	P0ABA0
SMRⁱ	P0ABA0
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4262109, 80 interactors
Database of interacting proteins More...DIPⁱ	DIP-35994N
IntActⁱ	P0ABA0, 2 interactors
STRINGⁱ	316385.ECDH10B_3923

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB03091 4-Amido-4-Carbamoyl-Butyric Acid

DrugBankⁱ

DB03091 4-Amido-4-Carbamoyl-Butyric Acid

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

TCDBⁱ

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

2D gel databases

SWISS-2DPAGEⁱ	P0ABA0

SWISS-2DPAGEⁱ

P0ABA0

Proteomic databases

EPDⁱ	P0ABA0
PaxDbⁱ	P0ABA0
PRIDEⁱ	P0ABA0

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC76759; AAC76759; b3736 BAE77552; BAE77552; BAE77552
GeneIDⁱ	948247
KEGGⁱ	ecj:JW3714 eco:b3736
PATRICⁱ	fig\|1411691.4.peg.2964

Organism-specific databases

EchoBASEⁱ	EB0101
EcoGeneⁱ	EG10103 atpF

Phylogenomic databases

eggNOGⁱ	ENOG4107Z6K Bacteria COG0711 LUCA
HOGENOMⁱ	HOG000015378
InParanoidⁱ	P0ABA0
KEGG Orthology (KO) More...KOⁱ	K02109
OMAⁱ	KFAWKPI
PhylomeDBⁱ	P0ABA0

Enzyme and pathway databases

BioCycⁱ	EcoCyc:ATPF-MONOMER MetaCyc:ATPF-MONOMER

BioCycⁱ

EcoCyc:ATPF-MONOMER
MetaCyc:ATPF-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P0ABA0
Protein Ontology More...PROⁱ	PR:P0ABA0

Family and domain databases

HAMAPⁱ	MF_01398 ATP_synth_b_bprime, 1 hit
InterProⁱ	View protein in InterPro IPR028987 ATP_synth_B-like_membr_sf IPR002146 ATP_synth_b/b'su_bac/chlpt IPR005864 ATP_synth_F0_bsu_bac
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00430 ATP-synt_B, 1 hit
SUPFAMⁱ	SSF81573 SSF81573, 1 hit
TIGRFAMsⁱ	TIGR01144 ATP_synt_b, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ATPF_ECOLI
Accessionⁱ	P0ABA0Primary (citable) accession number: P0ABA0 Secondary accession number(s): P00859, Q2M854
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
	Last sequence update:	July 21, 1986
	Last modified:	March 28, 2018
	This is version 107 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P0ABA0 (ATPF_ECOLI)

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ATP synthase subunit b

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

2D gel databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ