Skip Header

Contribute Send feedback
Read comments (?) or add your own

P43714 (ATPA_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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 alpha
EC=3.6.3.14
Alternative name(s):
ATP synthase F1 sector subunit alpha
F-ATPase subunit alpha
Gene names
Name:atpA
Ordered Locus Names:HI_0481
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length513 AA.
Sequence statusComplete.
Protein existenceInferred 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. 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 513513ATP synthase subunit alpha HAMAP MF_01346
PRO_0000144329

Regions

Nucleotide binding169 – 1768ATP By similarity

Sites

Site3731Required for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P43714 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 34B580C74524FA00

FASTA51355,591
        10         20         30         40         50         60 
MQLNSTEISE LIKKRIAQFD VVSEARNTGT IVSVSDGIIR IHGLSDVMQG EMIALPGNRY 

        70         80         90        100        110        120 
AMALNLERDS VGAVVMGPYA DLAEGMEVQC TGRILEVPVG RGLLGRVVNT LGQPIDGKGE 

       130        140        150        160        170        180 
IENDGFSPVE VIAPGVIDRR SVDQPVQTGY KAVDSMVPIG RGQRELIIGD RQTGKTALAI 

       190        200        210        220        230        240 
DAIINQRNSG IKCIYVAIGQ KASTIANVVR KLEEHGALAN TIVVAASASE SAALQYLAPY 

       250        260        270        280        290        300 
AGCAMGEYFR DRGEDALIVY DDLSKQAVAY RQISLLLRRP PGREAYPGDV FYLHSRLLER 

       310        320        330        340        350        360 
ASRVNEDYVE KFTKGEVKGK TGSLTALPII ETQAGDVSAF VPTNVISITD GQIFLESNLF 

       370        380        390        400        410        420 
NSGIRPAVNP GISVSRVGGS AQTKVIKKLA GGIRTALAQY RELAAFAQFA SDLDDATRKQ 

       430        440        450        460        470        480 
LSHGEKVTEL LKQKQFTPLS VAEQAVILFA VEFGYLDDVE LSKIASFETA LLDYSNRNHA 

       490        500        510 
EFMQELNKTG NYNDEIKDTL KSILDGFKAN SAW

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L42023 Genomic DNA. Translation: AAC22139.1.
PIRF64071.
RefSeqNP_438641.1. NC_000907.1.

3D structure databases

ProteinModelPortalP43714.
SMRP43714. Positions 29-507.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID950615.
GenomeReviewsGene locus HI_0481 in contig L42023_GR.
KEGGhin:HI0481.
NMPDRfig|71421.1.peg.454.
PATRIC20189515. VBIHaeInf48452_0500.
TIGRHI_0481.

Phylogenomic databases

HOGENOMHBG565875.
OMAFRVGIKA.
PhylomeDBP43714.
ProtClustDBPRK09281.

Enzyme and pathway databases

BioCycHINF71421:HI_0481-MONOMER.

Family and domain databases

HAMAPMF_01346. ATP_synth_alpha_bact.
[Tree]
InterProIPR020003. 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]
Gene3DG3DSA:2.40.30.20. G3DSA:2.40.30.20. 1 hit.
KOK02111.
PANTHERPTHR15184:SF3. ATPase_F1_a. 1 hit.
PfamPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SUPFAMSSF47917. ATPase_a/b_C. 1 hit.
SSF50615. ATPase_a/b_N. 1 hit.
TIGRFAMsTIGR00962. AtpA. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameATPA_HAEIN
AccessionPrimary (citable) accession number: P43714
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 25, 2012
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents