ATP synthase subunit alpha 2 - Legionella pneumophila (strain Paris)

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Q5X0P1 (ATPA2_LEGPA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
ATP synthase subunit alpha 2
EC=3.6.3.14

Alternative name(s):
ATP synthase F1 sector subunit alpha 2
F-ATPase subunit alpha 2

Gene names

Name:	atpA2
Ordered Locus Names:	lpp3055

Organism

Legionella pneumophila (strain Paris) [Complete proteome] [HAMAP]

Taxonomic identifier

297246 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Legionellaceae › Legionella

Protein attributes

Sequence length	517 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Cell inner membrane Cell membrane Membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
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	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell proton-transporting ATP synthase complex, catalytic core F(1) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 517

517

ATP synthase subunit alpha 2 HAMAP MF_01346

PRO_0000238271

Regions

Nucleotide binding

173 – 180

ATP By similarity

Sites

Site

377

Required for activity By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q5X0P1 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 406D720F0BC0A2F2
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FASTA

517

55,528

        10         20         30         40         50         60 
MSEQVALNPS EISELIRKKI DQFSVVSEAR NEGTIVSLKD GIVRLHGLAD VMAGEMIEFP 

        70         80         90        100        110        120 
GGVYGLALNL ERDSVGAVIL GDSSTLAEGQ KGKCTGRILE VPVGKGLLGR VVDALGNPID 

       130        140        150        160        170        180 
GKGPIESSGM SPIEKVAPGV ITRKSVDQPV QTGLKAIDAM IPVGRGQREL IIGDRQTGKT 

       190        200        210        220        230        240 
AIAIDAIINQ KGTGVKCVYV AIGQKASSVA SIVRKLEEHG ALEHTIVVVA GASDSAALQY 

       250        260        270        280        290        300 
IAPYSGCTMG EYFMERGEDA LIVYDDLTKQ AWAYRQISLL LRRPPGREAY PGDIFYLHSR 

       310        320        330        340        350        360 
LLERAARINA DEVEKLTNGE VKGKTGSLTA LPIIETQAGD VSAFVPTNVI SITDGQIFLD 

       370        380        390        400        410        420 
VDLFNSGVRP AINSGLSVSR VGGAAQTKIM KKLGGGTRLA LAQFRELEAF SQFASDLDDA 

       430        440        450        460        470        480 
TRKQLERGQR ITELMKQKQY SPLTVAEMGV SLFVVEKGYL DDVPVNEISS FEASLHDYMR 

       490        500        510 
STHAALLHAI NEAGAYDNEI EAKLKKAVEE FKNTGSW

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References

[1]

"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
Nat. Genet. 36:1165-1173(2004) [PubMed: 15467720] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Paris.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR628336 Genomic DNA. Translation: CAH14208.1.
RefSeq	YP_125357.1. NC_006368.1.
3D structure databases
ProteinModelPortal	Q5X0P1.
SMR	Q5X0P1. Positions 33-512.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5X0P1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3117604.
GenomeReviews	Gene locus lpp3055 in contig CR628336_GR.
KEGG	lpp:lpp3055.
PATRIC	22326859. VBILegPne27771_3458.
Organism-specific databases
LegioList	lpp3055.
CMR	Search...
Phylogenomic databases
eggNOG	COG0056.
HOGENOM	HBG565875.
OMA	GSDRDIK.
PhylomeDB	Q5X0P1.
ProtClustDB	PRK09281.
Enzyme and pathway databases
BioCyc	LPNE297246:LPP3055-MONOMER.
Family and domain databases
HAMAP	MF_01346. ATP_synth_alpha_bact. [Tree]
InterPro	IPR020003. 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]
Gene3D	G3DSA:2.40.30.20. G3DSA:2.40.30.20. 1 hit.
KO	K02111.
PANTHER	PTHR15184:SF3. ATPase_F1_a. 1 hit.
Pfam	PF00006. ATP-synt_ab. 1 hit. PF00306. ATP-synt_ab_C. 1 hit. PF02874. ATP-synt_ab_N. 1 hit. [Graphical view]
SUPFAM	SSF47917. ATPase_a/b_C. 1 hit. SSF50615. ATPase_a/b_N. 1 hit.
TIGRFAMs	TIGR00962. AtpA. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPA2_LEGPA

Accession

Primary (citable) accession number: Q5X0P1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	November 23, 2004
Last modified:	January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents