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Protein

ATP synthase subunit alpha

Gene

atpA

Organism
Escherichia coli O157:H7 (strain EC4115 / EHEC)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.UniRule annotation

Catalytic activityi

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei373Required for activityUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi169 – 176ATPUniRule annotation8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processATP synthesis, Hydrogen ion transport, Ion transport, Transport
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit alphaUniRule annotation (EC:3.6.3.14UniRule annotation)
Alternative name(s):
ATP synthase F1 sector subunit alphaUniRule annotation
F-ATPase subunit alphaUniRule annotation
Gene namesi
Name:atpAUniRule annotation
Ordered Locus Names:ECH74115_5170
OrganismiEscherichia coli O157:H7 (strain EC4115 / EHEC)
Taxonomic identifieri444450 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

Subcellular locationi

  • Cell inner membrane UniRule annotation; Peripheral membrane protein UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001433731 – 513ATP synthase subunit alphaAdd BLAST513

Proteomic databases

PRIDEiB5YXD8

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.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB5YXD8
SMRiB5YXD8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000130111
KOiK02111
OMAiGNAQIKS

Family and domain databases

CDDicd01132 F1_ATPase_alpha, 1 hit
Gene3Di1.20.150.20, 1 hit
2.40.30.20, 1 hit
HAMAPiMF_01346 ATP_synth_alpha_bact, 1 hit
InterProiView protein in InterPro
IPR023366 ATP_synth_asu-like_sf
IPR000793 ATP_synth_asu_C
IPR038376 ATP_synth_asu_C_sf
IPR033732 ATP_synth_F1_a
IPR005294 ATP_synth_F1_asu
IPR020003 ATPase_a/bsu_AS
IPR004100 ATPase_F1/V1/A1_a/bsu_N
IPR036121 ATPase_F1/V1/A1_a/bsu_N_sf
IPR000194 ATPase_F1/V1/A1_a/bsu_nucl-bd
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF00006 ATP-synt_ab, 1 hit
PF00306 ATP-synt_ab_C, 1 hit
PF02874 ATP-synt_ab_N, 1 hit
SUPFAMiSSF50615 SSF50615, 1 hit
SSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00962 atpA, 1 hit
PROSITEiView protein in PROSITE
PS00152 ATPASE_ALPHA_BETA, 1 hit

Sequencei

Sequence statusi: Complete.

B5YXD8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQLNSTEISE LIKQRIAQFN VVSEAHNEGT IVSVSDGVIR IHGLADCMQG
60 70 80 90 100
EMISLPGNRY AIALNLERDS VGAVVMGPYA DLAEGMKVKC TGRILEVPVG
110 120 130 140 150
RGLLGRVVNT LGAPIDGKGP LDHDGFSAVE AIAPGVIERQ SVDQPVQTGY
160 170 180 190 200
KAVDSMIPIG RGQRELIIGD RQTGKTALAI DAIINQRDSG IKCIYVAIGQ
210 220 230 240 250
KASTISNVVR KLEEHGALAN TIVVVATASE SAALQYLAPY AGCAMGEYFR
260 270 280 290 300
DRGEDALIIY DDLSKQAVAY RQISLLLRRP PGREAFPGDV FYLHSRLLER
310 320 330 340 350
AARVNAEYVE AFTKGEVKGK TGSLTALPII ETQAGDVSAF VPTNVISITD
360 370 380 390 400
GQIFLETNLF NAGIRPAVNP GISVSRVGGA AQTKIMKKLS GGIRTALAQY
410 420 430 440 450
RELAAFSQFA SDLDDATRKQ LDHGQKVTEL LKQKQYAPMS VAQQSLVLFA
460 470 480 490 500
AERGYLADVE LSKIGSFEAA LLAYVDRDHA PLMQEINQTG GYNDEIEGKL
510
KGILDSFKAT QSW
Length:513
Mass (Da):55,222
Last modified:November 25, 2008 - v1
Checksum:iDD1F3859375E9103
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001164 Genomic DNA Translation: ACI39451.1
RefSeqiWP_001176745.1, NC_011353.1

Genome annotation databases

EnsemblBacteriaiACI39451; ACI39451; ECH74115_5170
KEGGiecf:ECH74115_5170

Similar proteinsi

Entry informationi

Entry nameiATPA_ECO5E
AccessioniPrimary (citable) accession number: B5YXD8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 25, 2008
Last modified: March 28, 2018
This is version 68 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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