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Protein

Proteasome-associated ATPase

Gene

arc

Organism
Rhodococcus erythropolis (Arthrobacter picolinophilus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis.UniRule annotation2 Publications

Enzyme regulationi

ATPase activity is inhibited by N-ethylmaleimide (NEM) but not by sodium azide.1 Publication

Kineticsi

Is also able to cleave CTP at half the rate of ATP hydrolysis, but GTP or UTP are not substrates.

  1. KM=200 µM for ATP1 Publication
  1. Vmax=268 pmol/min/µg enzyme1 Publication

pH dependencei

Optimum pH is 7-8.1 Publication

Pathwayi: proteasomal Pup-dependent pathway

This protein is involved in the pathway proteasomal Pup-dependent pathway, which is part of Protein degradation.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway proteasomal Pup-dependent pathway and in Protein degradation.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi278 – 2836ATPUniRule annotation

GO - Molecular functioni

  • ATPase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-HAMAP
  • CTPase activity Source: UniProtKB

GO - Biological processi

  • modification-dependent protein catabolic process Source: UniProtKB-HAMAP
  • proteasomal protein catabolic process Source: UniProtKB
  • protein unfolding Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.4.8. 5389.
UniPathwayiUPA00997.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome-associated ATPaseUniRule annotation
Alternative name(s):
AAA ATPase forming ring-shaped complexesUniRule annotation
Short name:
ARCUniRule annotation
Proteasomal ATPaseUniRule annotation
Gene namesi
Name:arcUniRule annotation
OrganismiRhodococcus erythropolis (Arthrobacter picolinophilus)
Taxonomic identifieri1833 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesNocardiaceaeRhodococcus

Subcellular locationi

GO - Cellular componenti

  • proteasome-activating nucleotidase complex Source: UniProtKB
  • proteasome complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 591590Proteasome-associated ATPasePRO_0000383481Add
BLAST

Expressioni

Inductioni

Constitutively expressed.1 Publication

Interactioni

Subunit structurei

Homohexamer. Assembles into a hexameric ring structure that likely caps the 20S proteasome core. Can form a complex composed of two stacked hexameric rings in vitro. Probably interacts with the prokaryotic ubiquitin-like protein Pup through a hydrophobic interface; the expected interacting region of ARC lies in its N-terminal coiled-coil domain. There is likely one Pup binding site per ARC hexamer ring. Upon ATP-binding, the C-terminus of ARC probably interacts with the alpha-rings of the proteasome core, possibly by binding to the intersubunit pockets.UniRule annotation3 Publications

Protein-protein interaction databases

STRINGi234621.RER_31790.

Structurei

Secondary structure

1
591
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi80 – 889Combined sources
Beta strandi94 – 985Combined sources
Beta strandi101 – 1055Combined sources
Helixi113 – 1153Combined sources
Beta strandi121 – 1244Combined sources
Beta strandi130 – 1334Combined sources
Beta strandi139 – 14810Combined sources
Beta strandi152 – 1587Combined sources
Beta strandi164 – 1696Combined sources
Helixi171 – 1766Combined sources
Beta strandi201 – 2055Combined sources
Turni206 – 2094Combined sources
Beta strandi210 – 2156Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WFWX-ray1.60A/B/C73-225[»]
ProteinModelPortaliO50202.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO50202.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni590 – 5912Docks into pockets in the proteasome alpha-ringUniRule annotation

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili10 – 7768UniRule annotationAdd
BLAST

Domaini

Consists of three main regions, an N-terminal coiled-coil domain (residues 1-77) that probably binds to protein Pup and functions as a docking station, an interdomain (residues 78-227) involved in Mpa hexamerization, and a C-terminal ATPase domain of the AAA type (residues 228-533).1 Publication

Sequence similaritiesi

Belongs to the AAA ATPase family.UniRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG4105DHM. Bacteria.
COG0464. LUCA.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_02112. ARC_ATPase.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
IPR032501. Prot_ATP_ID_OB.
IPR022482. Proteasome_ATPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF16450. Prot_ATP_ID_OB. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
TIGRFAMsiTIGR03689. pup_AAA. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O50202-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSTENPDSV AAAEELHALR VEAQVLRRQL AQSPEQVREL ESKVDSLSIR
60 70 80 90 100
NSKLMDTLKE ARQQLIALRE EVDRLGQPPS GYGVLLSVHE DKTVDVFTSG
110 120 130 140 150
RKMRLTCSPN IDTDTLALGQ TVRLNEALTI VEAGTYEQVG EISTLREVLD
160 170 180 190 200
DGLRALVVGH ADEERIVWLA APLAAVFADP EADIIAYDAD SPTRKLRPGD
210 220 230 240 250
SLLVDTKAGY AFERIPKAEV EDLVLEEVPD VHYDDIGGLG RQIEQIRDAV
260 270 280 290 300
ELPFLHKDLF HEYSLRPPKG VLLYGPPGCG KTLIAKAVAN SLAKKIAEAR
310 320 330 340 350
GQDSKDAKSY FLNIKGPELL NKFVGETERH IRMIFQRARE KASEGTPVIV
360 370 380 390 400
FFDEMDSIFR TRGSGVSSDV ETTVVPQLLS EIDGVEGLEN VIVIGASNRE
410 420 430 440 450
DMIDPAILRP GRLDVKIKIE RPDAESAQDI FSKYLVDGLP INADDLAEFG
460 470 480 490 500
GDRTACLKAM IVRVVDRMYA ESEENRFLEV TYANGDKEVL FFKDFNSGAM
510 520 530 540 550
IQNIVDRAKK YAIKSVLDTG APGLRVQHLF DSIVDEFAEN EDLPNTTNPD
560 570 580 590
DWARISGKKG ERIVYIRTLV TGKNASASRA IDTESNTGQY L
Length:591
Mass (Da):65,354
Last modified:June 1, 1998 - v1
Checksum:i361FFFAB64F07A50
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF088800 Genomic DNA. Translation: AAC68690.1.
RefSeqiWP_003944870.1. NZ_LDPN01000083.1.

Genome annotation databases

GeneIDi7709372.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF088800 Genomic DNA. Translation: AAC68690.1.
RefSeqiWP_003944870.1. NZ_LDPN01000083.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WFWX-ray1.60A/B/C73-225[»]
ProteinModelPortaliO50202.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi234621.RER_31790.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi7709372.

Phylogenomic databases

eggNOGiENOG4105DHM. Bacteria.
COG0464. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00997.
BRENDAi3.6.4.8. 5389.

Miscellaneous databases

EvolutionaryTraceiO50202.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_02112. ARC_ATPase.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
IPR032501. Prot_ATP_ID_OB.
IPR022482. Proteasome_ATPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF16450. Prot_ATP_ID_OB. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
TIGRFAMsiTIGR03689. pup_AAA. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of ARC, a divergent member of the AAA ATPase family from Rhodococcus erythropolis."
    Wolf S., Nagy I., Lupas A., Pfeifer G., Cejka Z., Mueller S.A., Engel A., De Mot R., Baumeister W.
    J. Mol. Biol. 277:13-25(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, CLEAVAGE OF INITIATOR METHIONINE, FUNCTION AS AN ATPASE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, INDUCTION, SUBUNIT.
    Strain: NI86/21.
  2. "The N-terminal coiled coil of the Rhodococcus erythropolis ARC AAA ATPase is neither necessary for oligomerization nor nucleotide hydrolysis."
    Zhang X., Stoffels K., Wurzbacher S., Schoofs G., Pfeifer G., Banerjee T., Parret A.H., Baumeister W., De Mot R., Zwickl P.
    J. Struct. Biol. 146:155-165(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, SUBUNIT.
    Strain: NI86/21.
  3. "Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases."
    Djuranovic S., Hartmann M.D., Habeck M., Ursinus A., Zwickl P., Martin J., Lupas A.N., Zeth K.
    Mol. Cell 34:580-590(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 73-225, FUNCTION AS A CHAPERONE, SUBUNIT.

Entry informationi

Entry nameiARC_RHOER
AccessioniPrimary (citable) accession number: O50202
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: June 1, 1998
Last modified: July 6, 2016
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.