Q98QU0 (ATPL_MYCPU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	MYPU_2710

Organism

Mycoplasma pulmonis (strain UAB CTIP) [Complete proteome] [HAMAP]

Taxonomic identifier

272635 [NCBI]

Taxonomic lineage

Bacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Mycoplasma

Protein attributes

Sequence length	92 AA.
Sequence status	Complete.
Protein existence	Inferred 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 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 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 membrane; Multi-pass membrane protein By similarity HAMAP MF_01396.
Sequence similarities	Belongs to the ATPase C chain family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(0) Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Lipid-binding
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell proton-transporting ATP synthase complex, coupling factor F(o) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	hydrogen ion transmembrane transporter activity Inferred from electronic annotation. Source: InterPro lipid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 92	92	ATP synthase subunit c HAMAP MF_01396		PRO_0000365904
Regions
	Transmembrane	20 – 40	21	Helical; Potential
	Transmembrane	71 – 91	21	Helical; Potential
Sites
	Site	75	1	Reversibly protonated during proton transport By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q98QU0 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: 404C6417BE9BD8E0	FASTA	92	9,296
	10 20 30 40 50 60 MENIISLLAL KNDPTSATTG AGLVAVGAGL ASIGNFGTGL GQGLSAGRAA EAVGRNPEAI 70 80 90 KKIRSLMIIG MAISESASLY SFIIAILLVF VY

References

[1]

"The complete genome sequence of the murine respiratory pathogen Mycoplasma pulmonis." Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F., Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A. Nucleic Acids Res. 29:2145-2153(2001) [PubMed: 11353084] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: UAB CTIP.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL445563 Genomic DNA. Translation: CAC13444.1.
PIR	G90545.
RefSeq	NP_326102.1. NC_002771.1.
3D structure databases
HSSP	HSSP built from PDB template 1YCE based on UniProtKB Q8KRV3.
ProteinModelPortal	Q98QU0.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	911500.
GenomeReviews	Gene locus MYPU_2710 in contig AL445566_GR.
KEGG	mpu:MYPU_2710.
PATRIC	20023434. VBIMycPul29704_0274.
Organism-specific databases
GenoList	MYPU_2710.
CMR	Search...
Phylogenomic databases
HOGENOM	HBG753983.
OMA	CAITEST.
PhylomeDB	Q98QU0.
Enzyme and pathway databases
BioCyc	MPUL272635:MYPU_2710-MONOMER.
Family and domain databases
HAMAP	MF_01396. ATP_synth_c_bact. [Tree]
InterPro	IPR000454. ATPase_F0-cplx_csu. IPR005953. ATPase_F0-cplx_csu_bac/chlpt. IPR020537. ATPase_F0-cplx_csu_DDCD_BS. IPR002379. ATPase_F0/V0-cplx_csu. [Graphical view]
Gene3D	G3DSA:1.20.20.10. ATPase_F0/V0_c. 1 hit.
KO	K02110.
Pfam	PF00137. ATP-synt_C. 1 hit. [Graphical view]
PRINTS	PR00124. ATPASEC.
SUPFAM	SSF81333. ATPase_F0/V0_c. 1 hit.
TIGRFAMs	TIGR01260. ATP_synt_c. 1 hit.
PROSITE	PS00605. ATPASE_C. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPL_MYCPU

Accession

Primary (citable) accession number: Q98QU0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 3, 2009
Last sequence update:	October 1, 2001
Last modified:	January 25, 2012
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program