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Protein

ATP synthase subunit a

Gene

atpB

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

Functioni

Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.

Caution

Was originally proposed to be encoded from either Met-1 or Val-71 (PID CAA23521); it is now thought to start of Met-1.1 Publication

GO - Molecular functioni

  • proton-transporting ATP synthase activity, rotational mechanism Source: EcoCyc

GO - Biological processi

  • plasma membrane ATP synthesis coupled proton transport Source: EcoCyc

Keywordsi

Biological processATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:ATPB-MONOMER
MetaCyc:ATPB-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 subunit aUniRule annotation
Alternative name(s):
ATP synthase F0 sector subunit aUniRule annotation
F-ATPase subunit 6UniRule annotation
Gene namesi
Name:atpBUniRule annotation
Synonyms:papD, uncB
Ordered Locus Names:b3738, JW3716
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10099 atpB

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 39PeriplasmicCuratedAdd BLAST39
Transmembranei40 – 60HelicalCuratedAdd BLAST21
Topological domaini61 – 99CytoplasmicCuratedAdd BLAST39
Transmembranei100 – 120HelicalCuratedAdd BLAST21
Topological domaini121 – 145PeriplasmicCuratedAdd BLAST25
Transmembranei146 – 166HelicalCuratedAdd BLAST21
Topological domaini167 – 219CytoplasmicCuratedAdd BLAST53
Transmembranei220 – 240HelicalCuratedAdd BLAST21
Topological domaini241PeriplasmicCurated1
Transmembranei242 – 262HelicalCuratedAdd BLAST21
Topological domaini263 – 271CytoplasmicCurated9

GO - Cellular componenti

  • integral component of membrane Source: EcoliWiki
  • integral component of plasma membrane Source: EcoCyc
  • proton-transporting ATP synthase complex, coupling factor F(o) Source: EcoCyc

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi206S → L: Reduced activity. 1
Mutagenesisi207L → Y or F: No change in activity. 1
Mutagenesisi210R → K, I, V or E: Completely defective. 1
Mutagenesisi214N → H: Completely defective. 1
Mutagenesisi214N → V: Reduced activity. 1
Mutagenesisi217A → H: Reduced activity. 1
Mutagenesisi217A → R: Completely defective. 1
Mutagenesisi245H → Y: Reduced activity. 1

Chemistry databases

ChEMBLiCHEMBL1075074

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000820531 – 271ATP synthase subunit aAdd BLAST271

Proteomic databases

PaxDbiP0AB98
PRIDEiP0AB98

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: a1, b2 and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF1 is attached to CF0 by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains.

Protein-protein interaction databases

BioGridi4262600, 50 interactors
DIPiDIP-47956N
IntActiP0AB98, 2 interactors
MINTiP0AB98
STRINGi316385.ECDH10B_3925

Structurei

Secondary structure

1271
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi97 – 125Combined sources29
Helixi135 – 166Combined sources32
Helixi202 – 228Combined sources27
Beta strandi229 – 231Combined sources3
Helixi233 – 263Combined sources31

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C17NMR-M95-271[»]
5T4Oelectron microscopy6.90K1-271[»]
5T4Pelectron microscopy7.77K1-271[»]
5T4Qelectron microscopy8.53K1-271[»]
ProteinModelPortaliP0AB98
SMRiP0AB98
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AB98

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase A chain family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105EE4 Bacteria
COG0356 LUCA
HOGENOMiHOG000253872
InParanoidiP0AB98
KOiK02108
OMAiYRPWVPF
PhylomeDBiP0AB98

Family and domain databases

Gene3Di1.20.120.220, 1 hit
HAMAPiMF_01393 ATP_synth_a_bact, 1 hit
InterProiView protein in InterPro
IPR000568 ATP_synth_F0_asu
IPR023011 ATP_synth_F0_asu_AS
IPR035908 F0_ATP_A_sf
PfamiView protein in Pfam
PF00119 ATP-synt_A, 1 hit
PRINTSiPR00123 ATPASEA
SUPFAMiSSF81336 SSF81336, 1 hit
TIGRFAMsiTIGR01131 ATP_synt_6_or_A, 1 hit
PROSITEiView protein in PROSITE
PS00449 ATPASE_A, 1 hit

Sequencei

Sequence statusi: Complete.

P0AB98-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASENMTPQD YIGHHLNNLQ LDLRTFSLVD PQNPPATFWT INIDSMFFSV
60 70 80 90 100
VLGLLFLVLF RSVAKKATSG VPGKFQTAIE LVIGFVNGSV KDMYHGKSKL
110 120 130 140 150
IAPLALTIFV WVFLMNLMDL LPIDLLPYIA EHVLGLPALR VVPSADVNVT
160 170 180 190 200
LSMALGVFIL ILFYSIKMKG IGGFTKELTL QPFNHWAFIP VNLILEGVSL
210 220 230 240 250
LSKPVSLGLR LFGNMYAGEL IFILIAGLLP WWSQWILNVP WAIFHILIIT
260 270
LQAFIFMVLT IVYLSMASEE H
Length:271
Mass (Da):30,303
Last modified:July 21, 1986 - v1
Checksum:i4933EAF09401566D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti71V → M in CAA23521 (PubMed:6272190).Curated1
Sequence conflicti179 – 182TLQP → RCST in CAA23590 (PubMed:6277311).Curated4
Sequence conflicti188F → S in AAA24740 (PubMed:2874137).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01594 Genomic DNA Translation: AAA24731.1
X01631 Genomic DNA Translation: CAA25776.1
V00264 Genomic DNA Translation: CAA23514.1
V00266 Genomic DNA Translation: CAA23520.1
V00266 Genomic DNA Translation: CAA23521.1
V00310 Genomic DNA Translation: CAA23590.1
M25464 Genomic DNA Translation: AAA83869.2
M14019 Genomic DNA Translation: AAA24740.1
L10328 Genomic DNA Translation: AAA62090.1
U00096 Genomic DNA Translation: AAC76761.1
AP009048 Genomic DNA Translation: BAE77550.1
X01383 Genomic DNA Translation: CAA25641.1
M29174 Genomic DNA Translation: AAA24423.1
PIRiC93732 LWEC6
RefSeqiNP_418194.1, NC_000913.3
WP_000135625.1, NZ_CP014272.1

Genome annotation databases

EnsemblBacteriaiAAC76761; AAC76761; b3738
BAE77550; BAE77550; BAE77550
GeneIDi948252
KEGGiecj:JW3716
eco:b3738
PATRICifig|1411691.4.peg.2962

Similar proteinsi

Entry informationi

Entry nameiATP6_ECOLI
AccessioniPrimary (citable) accession number: P0AB98
Secondary accession number(s): P00855
, Q2M856, Q47065, Q47708
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: March 28, 2018
This is version 110 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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