ATP synthase subunit alpha 2 - Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / SLCC5334)

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A0ALL5 (ATPA2_LISW6) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 49. 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:	lwe2479

Organism

Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / SLCC5334) [Complete proteome] [HAMAP]

Taxonomic identifier

386043 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length	504 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 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 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 – 504

504

ATP synthase subunit alpha 2 HAMAP MF_01346

PRO_0000339038

Regions

Nucleotide binding

169 – 176

ATP By similarity

Sites

Site

362

Required for activity By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

A0ALL5 [UniParc].

Last modified November 28, 2006. Version 1.
Checksum: 02EA58BE846B4F40
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FASTA

504

55,106

        10         20         30         40         50         60 
MSIKAEEISS IIKQQIENYH SELKVSDVGT VTYIGDGIAR AHGLDNAMAG ELLEFSNGVM 

        70         80         90        100        110        120 
GMAQNLETND VGIIILGPYT EIREGDEVRR TGKIMEVPVG EALIGRVVNS LGQPVDGLGP 

       130        140        150        160        170        180 
IETTGTRPIE AVAPGVMQRQ SVNEPLQTGI KAIDALVPIG RGQRELIIGD RQTGKTSVAI 

       190        200        210        220        230        240 
DTILNQADQD MICIYVAIGQ KESTVRNAVE TLRHHGALDY TIVVTAAASQ PAPLLYLAPY 

       250        260        270        280        290        300 
AGVAMAEEFM YNGKHVLVVY DDLSKQAAAY RELSLLLRRP PGREAYPGDV FYLHSRLLER 

       310        320        330        340        350        360 
AAKLNDSLGG GSITALPFVE TQAGDISAYI PTNVISITDG QIFLQSDLFF SGVRPAINAG 

       370        380        390        400        410        420 
LSVSRVGGSA QIKAMKTVAG TLRLDLAAYR ELESFSQFGS DLDAATRAKL ERGKRTVEVL 

       430        440        450        460        470        480 
KQDLHKPLKV EKQVLILYAL VHKYLDDVPV HDVLRFESEM NTWFDHNRPE LLEEIRTTKK 

       490        500 
LPDEAKLEAA LKEFKNTFVP SEEK

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References

[1]

"Whole-genome sequence of Listeria welshimeri reveals common steps in genome reduction with Listeria innocua as compared to Listeria monocytogenes."
Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S., Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O., Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.

Chakraborty T.
J. Bacteriol. 188:7405-7415(2006) [PubMed: 16936040] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35897 / DSM 20650 / SLCC5334.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM263198 Genomic DNA. Translation: CAK21897.1.
RefSeq	YP_850676.1. NC_008555.1.
3D structure databases
ProteinModelPortal	A0ALL5.
SMR	A0ALL5. Positions 21-502.
ModBase	Search...
Protein-protein interaction databases
STRING	A0ALL5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4464984.
GenomeReviews	Gene locus lwe2479 in contig AM263198_GR.
KEGG	lwe:lwe2479.
NMPDR	fig\|386043.6.peg.2408.
PATRIC	20332215. VBILisWel39304_2488.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0056.
HOGENOM	HBG565875.
OMA	FRVGIKA.
PhylomeDB	A0ALL5.
ProtClustDB	PRK09281.
Enzyme and pathway databases
BioCyc	LWEL386043:LWE2479-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_LISW6

Accession

Primary (citable) accession number: A0ALL5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	November 28, 2006
Last modified:	December 14, 2011
This is version 49 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