P83483 (ATPBM_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit beta-1, mitochondrial
EC=3.6.3.14

Gene names

Ordered Locus Names:	At5g08670
ORF Names:	T2K12.11

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	556 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Catalytic activity	ATP + H2O + H+(In) = ADP + phosphate + H+(Out). UniProtKB P29685
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: a, b and c By similarity.
Subcellular location	Mitochondrion. Mitochondrion inner membrane. Note: Peripheral membrane protein. Ref.5 Ref.6
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) Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome Direct protein sequencing Reference 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 response to oxidative stress Inferred from direct assay. Source: TAIR
Cellular component	chloroplast Inferred from direct assay. Source: TAIR mitochondrial respiratory chain complex I Inferred from direct assay. Source: TAIR plasma membrane Inferred from direct assay. Source: TAIR vacuolar membrane Inferred from direct assay. Source: TAIR
Molecular function	ATP binding Inferred from direct assay. Source: TAIR cobalt ion binding Inferred from direct assay. Source: TAIR copper ion binding Inferred from direct assay. Source: TAIR 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 zinc ion binding Inferred from direct assay. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 51	51	Mitochondrion Ref.5
	Chain	52 – 556	505	ATP synthase subunit beta-1, mitochondrial Ref.5		PRO_0000002434
Regions
	Nucleotide binding	231 – 238	8	ATP By similarity UniProtKB P29685
Experimental info
	Sequence conflict	1	1	M → MTMITPSSNTTHYRESWYAC RYRSGIPGSTHASV in CAC81058. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P83483 [UniParc]. Last modified December 6, 2002. Version 1. Checksum: 1BF518B51D93E690	FASTA	556	59,671
	10 20 30 40 50 60 MASRRVLSSL LRSSSGRSAA KLGNRNPRLP SPSPARHAAP CSYLLGRVAE YATSSPASSA 70 80 90 100 110 120 APSSAPAKDE GKKTYDYGGK GAIGRVCQVI GAIVDVRFED QEGLPPIMTS LEVQDHPTRL 130 140 150 160 170 180 VLEVSHHLGQ NVVRTIAMDG TEGLVRGRKV LNTGAPITVP VGRATLGRIM NVLGEPIDER 190 200 210 220 230 240 GEIKTEHYLP IHRDAPALVD LATGQEILAT GIKVVDLLAP YQRGGKIGLF GGAGVGKTVL 250 260 270 280 290 300 IMELINNVAK AHGGFSVFAG VGERTREGND LYREMIESGV IKLGEKQSES KCALVYGQMN 310 320 330 340 350 360 EPPGARARVG LTGLTVAEYF RDAEGQDVLL FIDNIFRFTQ ANSEVSALLG RIPSAVGYQP 370 380 390 400 410 420 TLASDLGALQ ERITTTKKGS ITSVQAIYVP ADDLTDPAPA TTFAHLDATT VLSRQISELG 430 440 450 460 470 480 IYPAVDPLDS TSRMLSPHIL GEEHYNTARG VQKVLQNYKN LQDIIAILGM DELSEDDKLT 490 500 510 520 530 540 VARARKIQRF LSQPFHVAEI FTGAPGKYVD LKENINSFQG LLDGKYDDLS EQSFYMVGGI 550 DEVVAKAEKI AKESAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Mahon P. Thesis (2000), Cambridge University, United Kingdom Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(2000) [PubMed: 11130714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Functional annotation of a full-length Arabidopsis cDNA collection." Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K. Science 296:141-145(2002) [PubMed: 11910074] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Proteomic approach to identify novel mitochondrial proteins in Arabidopsis." Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P. Plant Physiol. 127:1694-1710(2001) [PubMed: 11743114] [Abstract] Cited for: PROTEIN SEQUENCE OF 52-66, SUBCELLULAR LOCATION. Tissue: Leaf and Stem.
[6]	"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins." Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H. Plant Cell 16:241-256(2004) [PubMed: 14671022] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. Strain: cv. Landsberg erecta.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ271468 mRNA. Translation: CAC81058.1. AL590346 Genomic DNA. Translation: CAC35872.1. AK118538 mRNA. Translation: BAC43141.1. AY054222 mRNA. Translation: AAL06882.1. AY080681 mRNA. Translation: AAL86357.1. AY113178 mRNA. Translation: AAM47481.1. AY117269 mRNA. Translation: AAM51344.1.
IPI	IPI00546068.
3D structure databases
ProteinModelPortal	P83483.
SMR	P83483. Positions 84-551.
ModBase	Search...
Protein-protein interaction databases
IntAct	P83483. 1 interaction.
MINT	MINT-4330205.
STRING	P83483.
Proteomic databases
PRIDE	P83483.
ProMEX	P83483.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GenomeReviews	Gene locus AT5G08670 in contig BA000015_GR.
Organism-specific databases
GeneFarm	2014. 157.
TAIR	At5g08670.
Phylogenomic databases
eggNOG	KOG1350.
HOGENOM	HBG565875.
InParanoid	P83483.
PhylomeDB	P83483.
Gene expression databases
Genevestigator	P83483.
GermOnline	AT5G08670. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR020971. ATP_synthase_F1_beta_su. 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.
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. PF11421. Synthase_beta. 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

ATPBM_ARATH

Accession

Primary (citable) accession number: P83483
Secondary accession number(s): Q541W7 , Q8VX26, Q9C5A8, Q9C5B0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	December 6, 2002
Last modified:	November 16, 2011
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program