ATP synthase subunit alpha 2 - Marinomonas sp. (strain MWYL1)

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A6W3T0 (ATPA2_MARMS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. 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:	Mmwyl1_4464

Organism

Marinomonas sp. (strain MWYL1) [Complete proteome] [HAMAP]

Taxonomic identifier

400668 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Marinomonas

Protein attributes

Sequence length	514 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 – 514

514

ATP synthase subunit alpha 2 HAMAP MF_01346

PRO_0000339040

Regions

Nucleotide binding

170 – 177

ATP By similarity

Sites

Site

374

Required for activity By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

A6W3T0 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 385156B47CE73CAA
Show »

FASTA

514

55,556

        10         20         30         40         50         60 
MQQLNPSEIS EIIKKRIENL DVSSDAQNEG TIVSVADGIV LIHGLADVMY GEMIEFPGGV 

        70         80         90        100        110        120 
YGIALNLERD SVGAVVLGKY QDLVEGQKVK CTGRILEVPI GPELLGRVVD ALGNPIDGKG 

       130        140        150        160        170        180 
AINAKLTDKV EKVAPGVIER QSVDQPIQTG YKAIDAMVPI GRGQRELIIG DRQIGKTALA 

       190        200        210        220        230        240 
IDTIIAQKDS GIKCVYVAIG QKQSTIANVV RKLEEAGAME YTTVVAAGAS DPAAMLYIAP 

       250        260        270        280        290        300 
YTGCTMGEYF RDRGEDALII YDDLTKQAWA YRQISLLLRR PPGREAYPGD VFYLHSRLLE 

       310        320        330        340        350        360 
RASRVNVDYV EKFTNGEVKG KTGSLTALPI IETQGGDVSA FVPTNVISIT DGQIFLETSS 

       370        380        390        400        410        420 
FNAGIRPAMN AGISVSRVGG AAQTKIVKKL GGGIRLALAQ YRELAAFAQF ASDLDEATRK 

       430        440        450        460        470        480 
QLEHGKQVTE LMKQKQFSPM SVADMGVVLY AANDGFLEDV ETSKIGSFET ALLSYMNSEH 

       490        500        510 
TDLMADINKT GNFNGEIEAT FKAAIEKFKA TQTW

« Hide

References

[1]

"Complete sequence of Marinomonas sp. MWYL1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.

Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MWYL1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000749 Genomic DNA. Translation: ABR73359.1.
RefSeq	YP_001343294.1. NC_009654.1.
3D structure databases
ProteinModelPortal	A6W3T0.
SMR	A6W3T0. Positions 25-511.
ModBase	Search...
Protein-protein interaction databases
STRING	A6W3T0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5367041.
GenomeReviews	Gene locus Mmwyl1_4464 in contig CP000749_GR.
KEGG	mmw:Mmwyl1_4464.
PATRIC	22472657. VBIMarSp124341_4632.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0056.
HOGENOM	HBG565875.
OMA	FRVGIKA.
Enzyme and pathway databases
BioCyc	MSP400668:MMWYL1_4464-MONOMER.
Family and domain databases
HAMAP	MF_01346. ATP_synth_alpha_bact. [Tree]
InterPro	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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPA2_MARMS

Accession

Primary (citable) accession number: A6W3T0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	August 21, 2007
Last modified:	January 25, 2012
This is version 45 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