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Protein

V-type ATP synthase beta chain

Gene

atpB

Organism
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal beta chain is a regulatory subunit.

Enzyme regulationi

Stimulated by sulfite, ethanol, glycerol, magnesium and zinc ions.

pH dependencei

Optimum pH is 5.2.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciMMAZ192952:GCK2-800-MONOMER.

Protein family/group databases

TCDBi3.A.2.3.1. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
V-type ATP synthase beta chain
Alternative name(s):
V-ATPase subunit B
Gene namesi
Name:atpB
Synonyms:ahaB
Ordered Locus Names:MM_0779
OrganismiMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Taxonomic identifieri192952 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
Proteomesi
  • UP000000595 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 460460V-type ATP synthase beta chainPRO_0000144657Add
BLAST

Interactioni

Subunit structurei

Composed of seven subunits; A, B, C, D, E, F and G.

Protein-protein interaction databases

STRINGi192952.MM_0779.

Structurei

Secondary structure

1
460
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 195Combined sources
Beta strandi29 – 335Combined sources
Beta strandi35 – 373Combined sources
Beta strandi39 – 479Combined sources
Beta strandi49 – 568Combined sources
Beta strandi58 – 603Combined sources
Beta strandi72 – 754Combined sources
Beta strandi77 – 804Combined sources
Helixi82 – 843Combined sources
Beta strandi88 – 903Combined sources
Beta strandi91 – 933Combined sources
Beta strandi95 – 984Combined sources
Beta strandi105 – 1128Combined sources
Turni113 – 1153Combined sources
Beta strandi124 – 1263Combined sources
Helixi132 – 1354Combined sources
Beta strandi148 – 1503Combined sources
Helixi156 – 16611Combined sources
Beta strandi170 – 1745Combined sources
Beta strandi176 – 18510Combined sources
Helixi187 – 20014Combined sources
Helixi202 – 2054Combined sources
Beta strandi206 – 2127Combined sources
Helixi217 – 23822Combined sources
Beta strandi241 – 2477Combined sources
Helixi249 – 2568Combined sources
Helixi260 – 2623Combined sources
Helixi275 – 28410Combined sources
Beta strandi288 – 2903Combined sources
Beta strandi296 – 3049Combined sources
Turni309 – 3113Combined sources
Helixi318 – 3214Combined sources
Beta strandi324 – 3285Combined sources
Helixi330 – 3345Combined sources
Turni343 – 3453Combined sources
Helixi351 – 3533Combined sources
Turni357 – 3593Combined sources
Helixi364 – 38825Combined sources
Helixi390 – 3923Combined sources
Helixi395 – 41016Combined sources
Helixi422 – 43312Combined sources
Helixi438 – 4403Combined sources
Helixi446 – 4527Combined sources
Turni454 – 4563Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C61X-ray1.50A/B1-460[»]
2RKWX-ray2.81A/B1-460[»]
3B2QX-ray2.10A/B1-460[»]
3DSRX-ray2.70A/B1-460[»]
3EIUX-ray3.43A/B1-460[»]
3SSAX-ray1.70A/B1-460[»]
3TGWX-ray1.75A/B1-460[»]
3TIVX-ray1.75A/B1-460[»]
ProteinModelPortaliQ60187.
SMRiQ60187. Positions 13-456.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60187.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Phylogenomic databases

eggNOGiarCOG00865. Archaea.
COG1156. LUCA.
HOGENOMiHOG000165320.
KOiK02118.
OMAiNEEAQYF.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00310. ATP_synth_B_arch. 1 hit.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR005724. ATPase_A1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR027417. P-loop_NTPase.
IPR022879. V-ATPase_su_B/beta.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
PIRSFiPIRSF039114. V-ATPsynth_beta/V-ATPase_B. 1 hit.
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01041. ATP_syn_B_arch. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q60187-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKEYKTITQ IAGPLIFVEK TEPVGYNEIV NIKMGDGTVR RGQVLDSSAD
60 70 80 90 100
IVVVQVFEGT GGLDKDCGVI FTGETLKLPA SVDLLGRILS GSGEPRDGGP
110 120 130 140 150
RIVPDQLLDI NGAAMNPYAR LPPKDFIQTG ISTIDGTNTL VRGQKLPIFS
160 170 180 190 200
ASGLPHNEIA LQIARQASVP GSESAFAVVF AAMGITNEEA QYFMSDFEKT
210 220 230 240 250
GALERAVVFL NLADDPAVER IVTPRMALTA AEYLAYEHGM HVLVILTDIT
260 270 280 290 300
NYAEALRQMG AARNEVPGRR GYPGYMYTDL ATLYERAGIV KGAKGSVTQI
310 320 330 340 350
PILSMPGDDI THPIPDLSGY ITEGQIVVAR ELHRKGIYPP INVLPSLSRL
360 370 380 390 400
MNSGIGAGKT REDHKAVSDQ MYAGYAEGRD LRGLVAIVGK EALSERDTKF
410 420 430 440 450
LEFADLFEDK FVRQGRNENR TIEDTLEIGW QILTHLPENQ LGRIDNKYIQ
460
KYHPAHRKAK
Length:460
Mass (Da):50,282
Last modified:July 26, 2002 - v2
Checksum:i3A7E6BD8ECBB5A7F
GO

Sequence cautioni

The sequence AAM30475 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → V in AAC06376 (PubMed:8702544).Curated
Sequence conflicti49 – 6820ADIVV…DKDCG → LTLWLSRFSKVLVGLTRTAV in AAC06376 (PubMed:8702544).CuratedAdd
BLAST
Sequence conflicti90 – 901S → F in AAC06376 (PubMed:8702544).Curated
Sequence conflicti215 – 2151D → E in AAC06376 (PubMed:8702544).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U47274 Genomic DNA. Translation: AAC06376.1.
AE008384 Genomic DNA. Translation: AAM30475.1. Different initiation.
PIRiT45108.
RefSeqiWP_015411348.1. NC_003901.1.

Genome annotation databases

EnsemblBacteriaiAAM30475; AAM30475; MM_0779.
GeneIDi24880418.
KEGGimma:MM_0779.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U47274 Genomic DNA. Translation: AAC06376.1.
AE008384 Genomic DNA. Translation: AAM30475.1. Different initiation.
PIRiT45108.
RefSeqiWP_015411348.1. NC_003901.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C61X-ray1.50A/B1-460[»]
2RKWX-ray2.81A/B1-460[»]
3B2QX-ray2.10A/B1-460[»]
3DSRX-ray2.70A/B1-460[»]
3EIUX-ray3.43A/B1-460[»]
3SSAX-ray1.70A/B1-460[»]
3TGWX-ray1.75A/B1-460[»]
3TIVX-ray1.75A/B1-460[»]
ProteinModelPortaliQ60187.
SMRiQ60187. Positions 13-456.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi192952.MM_0779.

Protein family/group databases

TCDBi3.A.2.3.1. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM30475; AAM30475; MM_0779.
GeneIDi24880418.
KEGGimma:MM_0779.

Phylogenomic databases

eggNOGiarCOG00865. Archaea.
COG1156. LUCA.
HOGENOMiHOG000165320.
KOiK02118.
OMAiNEEAQYF.

Enzyme and pathway databases

BioCyciMMAZ192952:GCK2-800-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ60187.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00310. ATP_synth_B_arch. 1 hit.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR005724. ATPase_A1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR027417. P-loop_NTPase.
IPR022879. V-ATPase_su_B/beta.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
PIRSFiPIRSF039114. V-ATPsynth_beta/V-ATPase_B. 1 hit.
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01041. ATP_syn_B_arch. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVATB_METMA
AccessioniPrimary (citable) accession number: Q60187
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 26, 2002
Last modified: September 7, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.