Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q5FRC7 (ATPA1_GLUOX) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase subunit alpha 1
EC=3.6.3.14
Alternative name(s):
ATP synthase F1 sector subunit alpha 1
F-ATPase subunit alpha 1
Gene names
Name:atpA1
Ordered Locus Names:GOX1311
OrganismGluconobacter oxydans (strain 621H) (Gluconobacter suboxydans) [Complete proteome] [HAMAP]
Taxonomic identifier290633 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Gluconobacter

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit By similarity. HAMAP MF_01346

Catalytic activity

ATP + H2O + H+(In) = ADP + phosphate + H+(Out). HAMAP MF_01346

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: 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 By similarity.

Subcellular location

Cell inner membrane; Peripheral membrane protein By similarity HAMAP MF_01346.

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 511511ATP synthase subunit alpha 1 HAMAP MF_01346
PRO_0000238258

Regions

Nucleotide binding170 – 1778ATP By similarity

Sites

Site3711Required for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5FRC7 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: ACBC5BEE20FD3F8F

FASTA51154,952
        10         20         30         40         50         60 
MDIRPAEISD ILKQQIASFD QVETVSETGT VLSIGDGIAR VYGLTNVMAG EMVEFEGTGL 

        70         80         90        100        110        120 
KGMALNLEAD NVGVVLFGDG DSIREGDTVL RTKSVVEVPV GKGLLGRVVD GLGNPIDGRG 

       130        140        150        160        170        180 
PLTDVEYRRA EVKAPGIMPR QSVSEPMQTG IKAIDALVPI GRGQRELIIG DRQTGKTAIL 

       190        200        210        220        230        240 
IDTIVAQKPV NAEGDPKKSL YCIYVAVGQK RSTVANLVRT LIEHGAMEYS IVVAATASDA 

       250        260        270        280        290        300 
APMQYLAPYT ACAMGEYFRD NGMHALVCYD DLSKQAVAYR QMSLLLRRPP AREAFPGDVF 

       310        320        330        340        350        360 
YLHSRLLERA AKMSDANGGG SLTALPVIET QAGDTAAYIP TNVISITDGQ IFLETDLFYR 

       370        380        390        400        410        420 
GIRPAVNVGG SVSRVGSAAQ IKAMKQVAGK IKLELAQYRE MAAFSQFASD LDAATRKQLD 

       430        440        450        460        470        480 
RGARLVELLK QPETSPLPVE EQVVVLYAGT RGYVDPIAVD KVVAYEAALL SELRGAGSDI 

       490        500        510 
LTAIRNDRQI KPETEGKLKE LLEAFGKRFS A

« Hide

References

[1]"Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans."
Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., Ehrenreich A., Gottschalk G., Deppenmeier U.
Nat. Biotechnol. 23:195-200(2005) [PubMed: 15665824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 621H.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000009 Genomic DNA. Translation: AAW61069.1.
RefSeqYP_191725.1. NC_006677.1.

3D structure databases

ProteinModelPortalQ5FRC7.
SMRQ5FRC7. Positions 25-502.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3250774.
GenomeReviewsGene locus GOX1311 in contig CP000009_GR.
KEGGgox:GOX1311.
NMPDRfig|290633.1.peg.1270.
PATRIC32610432. VBIGluOxy81109_1574.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG565875.
OMAGSDRDIK.
ProtClustDBPRK09281.

Enzyme and pathway databases

BioCycGOXY290633:GOX1311-MONOMER.

Family and domain databases

HAMAPMF_01346. ATP_synth_alpha_bact.
[Tree]
InterProIPR020003. ATPase_a/bsu_AS.
IPR005294. ATPase_F1-cplx_asu.
IPR018118. ATPase_F1/A1-cplx_a/bsu_N.
IPR023366. ATPase_F1/A1-cplx_a_su_N.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR004100. ATPase_F1/V1/A1-cplx_a/bsu_N.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
[Graphical view]
Gene3DG3DSA:2.40.30.20. G3DSA:2.40.30.20. 1 hit.
KOK02111.
PANTHERPTHR15184:SF3. ATPase_F1_a. 1 hit.
PfamPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SUPFAMSSF47917. ATPase_a/b_C. 1 hit.
SSF50615. ATPase_a/b_N. 1 hit.
TIGRFAMsTIGR00962. AtpA. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameATPA1_GLUOX
AccessionPrimary (citable) accession number: Q5FRC7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: March 1, 2005
Last modified: January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents