ATP synthase subunit beta 1 - Mycoplasma pulmonis (strain UAB CTIP)

Contribute

Send feedback

Read comments (?) or add your own

Q98QU5 (ATPB1_MYCPU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 75. History...

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

Documents (1) |

Third-party data

text xml rdf/xml gff fasta

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 beta 1
EC=3.6.3.14

Alternative name(s):
ATP synthase F1 sector subunit beta 1
F-ATPase subunit beta 1

Gene names

Name:	atpD1
Ordered Locus Names:	MYPU_2660

Organism

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

Taxonomic identifier

272635 [NCBI]

Taxonomic lineage

Bacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Mycoplasma

Protein attributes

Sequence length	475 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 catalytic sites are hosted primarily by the beta subunits By similarity. HAMAP MF_01347
Catalytic activity	ATP + H₂O + H⁺(In) = ADP + phosphate + H⁺(Out). HAMAP MF_01347
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_01347.
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 hydrogen-exporting ATPase activity, phosphorylative 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 – 475

475

ATP synthase subunit beta 1 HAMAP MF_01347

PRO_0000254308

Regions

Nucleotide binding

153 – 160

ATP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q98QU5 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 363793DE94B20FD7
Show »

FASTA

475

51,864

        10         20         30         40         50         60 
MSQKNVGKIV QILGPVVDIS FAGQKIPAIY NNLELVFENN KYNFEVAQHI GDEVVRTISM 

        70         80         90        100        110        120 
VSTNGLSRGL EVIDTGAPIM VPVGKEVLSR MFNVLGQTID NKGEIEAKEF RSIHASAPSY 

       130        140        150        160        170        180 
EEQNDSSEIL ETGIKVIDLL VPYSKGGKIG LFGGAGVGKT VLVQELINNI ATQHGGLSVF 

       190        200        210        220        230        240 
AGVGERTREG NDLYHEMIAS GVLDKTTLVF GQMNEPPGAR MRVALTGLTM AEYFRDKFKQ 

       250        260        270        280        290        300 
DVLLFIDNIF RFTQAGSEVS ALLGRMPSAV GYQPTLATEM GQLQERITST KNGSITSVQA 

       310        320        330        340        350        360 
VYVPADDLTD PAPATTFTHL DAKTVLERNI AALGIYPAID PLASSSRMLD PLIIGNEHYL 

       370        380        390        400        410        420 
VALEVQNILQ RFKELQDIIA ILGIGELSEE DKKLVFRARK IRNFLSQPFT VAEKFSGKKG 

       430        440        450        460        470 
KFVPLKETIR SFKEILEGKH DNLPEDAFLY VGSIDEAIEK AKGQSNATTA NNNNA

« Hide

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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL445563 Genomic DNA. Translation: CAC13439.1.
PIR	B90545.
RefSeq	NP_326097.1. NC_002771.1.
3D structure databases
HSSP	HSSP built from PDB template 1SKY based on UniProtKB P07677.
ProteinModelPortal	Q98QU5.
SMR	Q98QU5. Positions 5-462.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	911682.
GenomeReviews	Gene locus MYPU_2660 in contig AL445566_GR.
KEGG	mpu:MYPU_2660.
PATRIC	20023424. VBIMycPul29704_0269.
Organism-specific databases
GenoList	MYPU_2660.
CMR	Search...
Phylogenomic databases
HOGENOM	HBG565875.
OMA	IGQEHYD.
PhylomeDB	Q98QU5.
ProtClustDB	PRK09280.
Enzyme and pathway databases
BioCyc	MPUL272635:MYPU_2660-MONOMER.
Family and domain databases
HAMAP	MF_01347. ATP_synth_beta_bact. [Tree]
InterPro	IPR020003. ATPase_a/bsu_AS. IPR003593. ATPase_AAA+_core. IPR005722. ATPase_F1-cplx_bsu. IPR018118. ATPase_F1/A1-cplx_a/bsu_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. IPR024034. ATPase_F1_bsu/V1_C. [Graphical view]
Gene3D	G3DSA:1.10.1140.10. G3DSA:1.10.1140.10. 1 hit.
KO	K02112.
PANTHER	PTHR15184:SF8. ATPase_F1_b. 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]
SMART	SM00382. AAA. 1 hit. [Graphical view]
SUPFAM	SSF47917. ATPase_a/b_C. 1 hit. SSF50615. ATPase_a/b_N. 1 hit.
TIGRFAMs	TIGR01039. AtpD. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPB1_MYCPU

Accession

Primary (citable) accession number: Q98QU5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	October 1, 2001
Last modified:	January 25, 2012
This is version 75 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

Sequences

References

Cross-references

Sequence databases

3D structure 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