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Q2LRB9 (ATPL_SYNAS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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

Names and origin

Protein namesRecommended name:
ATP synthase subunit c
Alternative name(s):
ATP synthase F(0) sector subunit c
F-type ATPase subunit c
Short name=F-ATPase subunit c
Lipid-binding protein
Gene names
Name:atpE
Ordered Locus Names:SYNAS_07470
ORF Names:SYN_02965
OrganismSyntrophus aciditrophicus (strain SB) [Complete proteome] [HAMAP]
Taxonomic identifier56780 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaSyntrophobacteralesSyntrophaceaeSyntrophus

Protein attributes

Sequence length118 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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-Rule MF_01396

Key component of the F0 channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F1 delta and epsilon subunits By similarity. HAMAP-Rule MF_01396

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.

Subcellular location

Cell inner membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_01396.

Sequence similarities

Belongs to the ATPase C chain family.

Sequence caution

The sequence ABC76626.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 118118ATP synthase subunit c HAMAP-Rule MF_01396
PRO_0000365932

Regions

Transmembrane34 – 5421Helical; Potential
Transmembrane88 – 10821Helical; Potential

Sites

Site921Reversibly protonated during proton transport By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2LRB9 [UniParc].

Last modified March 3, 2009. Version 2.
Checksum: F43F00818D52803C

FASTA11811,534
        10         20         30         40         50         60 
MVTCLTTFAV LLLTAAVASA AEAAAPGGES YVKAIFAVGA MIGAGIAIGV GAVGAGLGIG 

        70         80         90        100        110 
TAASGACQAV GRNPGVQGKI MMTMLVGMAM AESIAIYALV VSLVLIFANP YTKFFFVG 

« Hide

References

[1]"The genome of the syntrophic bacterium Syntrophus aciditrophicus: Life dependent on negative change in electrical potential."
Gunsalus R., Rohlin L., Kim U., Krupp R., Bhattacharyya A., Campbell J., Mclerney M., Moutakki H., Rio-Hernandez L.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000252 Genomic DNA. Translation: ABC76626.1. Different initiation.
RefSeqYP_460794.1. NC_007759.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING56780.SYN_02965.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC76626; ABC76626; SYN_02965.
GeneID3885232.
KEGGsat:SYN_02965.
PATRIC23861997. VBISynAci70500_0809.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG283790.
HOGENOMHOG000235245.
KOK02110.
OrthoDBEOG68H8G3.

Enzyme and pathway databases

BioCycSACI56780:GHXT-768-MONOMER.

Family and domain databases

Gene3D1.20.20.10. 1 hit.
HAMAPMF_01396. ATP_synth_c_bact.
InterProIPR000454. ATPase_F0-cplx_csu.
IPR005953. ATPase_F0-cplx_csu_bac/chlpt.
IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
IPR002379. ATPase_proteolipid_c_like_dom.
[Graphical view]
PfamPF00137. ATP-synt_C. 1 hit.
[Graphical view]
PRINTSPR00124. ATPASEC.
SUPFAMSSF81333. SSF81333. 1 hit.
TIGRFAMsTIGR01260. ATP_synt_c. 1 hit.
PROSITEPS00605. ATPASE_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameATPL_SYNAS
AccessionPrimary (citable) accession number: Q2LRB9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 60 of the entry and version 2 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