ARC_RHOER
ID ARC_RHOER Reviewed; 591 AA.
AC O50202;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Proteasome-associated ATPase {ECO:0000255|HAMAP-Rule:MF_02112};
DE AltName: Full=AAA ATPase forming ring-shaped complexes {ECO:0000255|HAMAP-Rule:MF_02112};
DE Short=ARC {ECO:0000255|HAMAP-Rule:MF_02112};
DE AltName: Full=Proteasomal ATPase {ECO:0000255|HAMAP-Rule:MF_02112};
GN Name=arc {ECO:0000255|HAMAP-Rule:MF_02112};
OS Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC Rhodococcus erythropolis group.
OX NCBI_TaxID=1833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, CLEAVAGE
RP OF INITIATOR METHIONINE, FUNCTION AS AN ATPASE, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, INDUCTION, AND SUBUNIT.
RC STRAIN=NI86/21;
RX PubMed=9514743; DOI=10.1006/jmbi.1997.1589;
RA Wolf S., Nagy I., Lupas A., Pfeifer G., Cejka Z., Mueller S.A., Engel A.,
RA De Mot R., Baumeister W.;
RT "Characterization of ARC, a divergent member of the AAA ATPase family from
RT Rhodococcus erythropolis.";
RL J. Mol. Biol. 277:13-25(1998).
RN [2]
RP DOMAIN, AND SUBUNIT.
RC STRAIN=NI86/21;
RX PubMed=15037247; DOI=10.1016/j.jsb.2003.10.020;
RA Zhang X., Stoffels K., Wurzbacher S., Schoofs G., Pfeifer G., Banerjee T.,
RA Parret A.H., Baumeister W., De Mot R., Zwickl P.;
RT "The N-terminal coiled coil of the Rhodococcus erythropolis ARC AAA ATPase
RT is neither necessary for oligomerization nor nucleotide hydrolysis.";
RL J. Struct. Biol. 146:155-165(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 73-225, FUNCTION AS A CHAPERONE,
RP AND SUBUNIT.
RX PubMed=19481487; DOI=10.1016/j.molcel.2009.04.030;
RA Djuranovic S., Hartmann M.D., Habeck M., Ursinus A., Zwickl P., Martin J.,
RA Lupas A.N., Zeth K.;
RT "Structure and activity of the N-terminal substrate recognition domains in
RT proteasomal ATPases.";
RL Mol. Cell 34:580-590(2009).
CC -!- FUNCTION: ATPase which is responsible for recognizing, binding,
CC unfolding and translocation of pupylated proteins into the bacterial
CC 20S proteasome core particle. May be essential for opening the gate of
CC the 20S proteasome via an interaction with its C-terminus, thereby
CC allowing substrate entry and access to the site of proteolysis. Thus,
CC the C-termini of the proteasomal ATPase may function like a 'key in a
CC lock' to induce gate opening and therefore regulate proteolysis.
CC {ECO:0000255|HAMAP-Rule:MF_02112, ECO:0000269|PubMed:19481487,
CC ECO:0000269|PubMed:9514743}.
CC -!- ACTIVITY REGULATION: ATPase activity is inhibited by N-ethylmaleimide
CC (NEM) but not by sodium azide. {ECO:0000269|PubMed:9514743}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=200 uM for ATP {ECO:0000269|PubMed:9514743};
CC Vmax=268 pmol/min/ug enzyme {ECO:0000269|PubMed:9514743};
CC Note=Is also able to cleave CTP at half the rate of ATP hydrolysis,
CC but GTP or UTP are not substrates.;
CC pH dependence:
CC Optimum pH is 7-8. {ECO:0000269|PubMed:9514743};
CC -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC {ECO:0000255|HAMAP-Rule:MF_02112}.
CC -!- SUBUNIT: Homohexamer. Assembles into a hexameric ring structure that
CC likely caps the 20S proteasome core. Can form a complex composed of two
CC stacked hexameric rings in vitro. Probably interacts with the
CC prokaryotic ubiquitin-like protein Pup through a hydrophobic interface;
CC the expected interacting region of ARC lies in its N-terminal coiled-
CC coil domain. There is likely one Pup binding site per ARC hexamer ring.
CC Upon ATP-binding, the C-terminus of ARC probably interacts with the
CC alpha-rings of the proteasome core, possibly by binding to the
CC intersubunit pockets. {ECO:0000255|HAMAP-Rule:MF_02112,
CC ECO:0000269|PubMed:15037247, ECO:0000269|PubMed:19481487,
CC ECO:0000269|PubMed:9514743}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:9514743}.
CC -!- DOMAIN: Consists of three main regions, an N-terminal coiled-coil
CC domain (residues 1-77) that probably binds to protein Pup and functions
CC as a docking station, an interdomain (residues 78-227) involved in Mpa
CC hexamerization, and a C-terminal ATPase domain of the AAA type
CC (residues 228-533). {ECO:0000269|PubMed:15037247}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000255|HAMAP-
CC Rule:MF_02112}.
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DR EMBL; AF088800; AAC68690.1; -; Genomic_DNA.
DR RefSeq; WP_003944870.1; NZ_UGVH01000001.1.
DR PDB; 2WFW; X-ray; 1.60 A; A/B/C=73-225.
DR PDBsum; 2WFW; -.
DR AlphaFoldDB; O50202; -.
DR SMR; O50202; -.
DR STRING; 1833.XU06_14825; -.
DR GeneID; 64141013; -.
DR OMA; CVDEFKE; -.
DR BRENDA; 5.6.1.5; 5389.
DR UniPathway; UPA00997; -.
DR EvolutionaryTrace; O50202; -.
DR GO; GO:0000502; C:proteasome complex; IGC:UniProtKB.
DR GO; GO:0022623; C:proteasome-activating nucleotidase complex; IGC:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0043273; F:CTPase activity; IDA:UniProtKB.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IEA:InterPro.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IGC:UniProtKB.
DR Gene3D; 2.40.50.140; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_02112; ARC_ATPase; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_C.
DR InterPro; IPR041626; Prot_ATP_ID_OB_N.
DR InterPro; IPR022482; Proteasome_ATPase.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR Pfam; PF17758; Prot_ATP_OB_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03689; pup_AAA; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Coiled coil;
KW Direct protein sequencing; Nucleotide-binding; Proteasome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9514743"
FT CHAIN 2..591
FT /note="Proteasome-associated ATPase"
FT /id="PRO_0000383481"
FT REGION 590..591
FT /note="Docks into pockets in the proteasome alpha-ring"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT COILED 10..77
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT BINDING 278..283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:2WFW"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:2WFW"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:2WFW"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:2WFW"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:2WFW"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:2WFW"
FT STRAND 139..148
FT /evidence="ECO:0007829|PDB:2WFW"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:2WFW"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:2WFW"
FT HELIX 171..176
FT /evidence="ECO:0007829|PDB:2WFW"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:2WFW"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:2WFW"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:2WFW"
SQ SEQUENCE 591 AA; 65354 MW; 361FFFAB64F07A50 CRC64;
MSSTENPDSV AAAEELHALR VEAQVLRRQL AQSPEQVREL ESKVDSLSIR NSKLMDTLKE
ARQQLIALRE EVDRLGQPPS GYGVLLSVHE DKTVDVFTSG RKMRLTCSPN IDTDTLALGQ
TVRLNEALTI VEAGTYEQVG EISTLREVLD DGLRALVVGH ADEERIVWLA APLAAVFADP
EADIIAYDAD SPTRKLRPGD SLLVDTKAGY AFERIPKAEV EDLVLEEVPD VHYDDIGGLG
RQIEQIRDAV ELPFLHKDLF HEYSLRPPKG VLLYGPPGCG KTLIAKAVAN SLAKKIAEAR
GQDSKDAKSY FLNIKGPELL NKFVGETERH IRMIFQRARE KASEGTPVIV FFDEMDSIFR
TRGSGVSSDV ETTVVPQLLS EIDGVEGLEN VIVIGASNRE DMIDPAILRP GRLDVKIKIE
RPDAESAQDI FSKYLVDGLP INADDLAEFG GDRTACLKAM IVRVVDRMYA ESEENRFLEV
TYANGDKEVL FFKDFNSGAM IQNIVDRAKK YAIKSVLDTG APGLRVQHLF DSIVDEFAEN
EDLPNTTNPD DWARISGKKG ERIVYIRTLV TGKNASASRA IDTESNTGQY L
