ARC_NAKMY
ID ARC_NAKMY Reviewed; 592 AA.
AC C8XAR0;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
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}; OrderedLocusNames=Namu_2975;
OS Nakamurella multipartita (strain ATCC 700099 / DSM 44233 / CIP 104796 / JCM
OS 9543 / NBRC 105858 / Y-104) (Microsphaera multipartita).
OC Bacteria; Actinobacteria; Nakamurellales; Nakamurellaceae; Nakamurella.
OX NCBI_TaxID=479431;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700099 / DSM 44233 / CIP 104796 / JCM 9543 / NBRC 105858 /
RC Y-104;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Sims D., Meincke L., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Nakamurella multipartita DSM 44233.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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 caps the 20S proteasome core. Strongly interacts with the prokaryotic
CC ubiquitin-like protein Pup through a hydrophobic interface; the
CC interacting region of ARC lies in its N-terminal coiled-coil domain.
CC There is one Pup binding site per ARC hexamer ring. Upon ATP-binding,
CC the C-terminus of ARC interacts with the alpha-rings of the proteasome
CC core, possibly by binding to the intersubunit pockets.
CC {ECO:0000255|HAMAP-Rule:MF_02112}.
CC -!- DOMAIN: Consists of three main regions, an N-terminal coiled-coil
CC domain that binds to protein Pup and functions as a docking station, an
CC interdomain involved in ARC hexamerization, and a C-terminal ATPase
CC domain of the AAA type. {ECO:0000255|HAMAP-Rule:MF_02112}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000255|HAMAP-
CC Rule:MF_02112}.
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DR EMBL; CP001737; ACV79313.1; -; Genomic_DNA.
DR AlphaFoldDB; C8XAR0; -.
DR SMR; C8XAR0; -.
DR STRING; 479431.Namu_2975; -.
DR EnsemblBacteria; ACV79313; ACV79313; Namu_2975.
DR KEGG; nml:Namu_2975; -.
DR eggNOG; COG1222; Bacteria.
DR HOGENOM; CLU_036054_0_0_11; -.
DR OMA; CVDEFKE; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000002218; Chromosome.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IEA:InterPro.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IEA:InterPro.
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 3: Inferred from homology;
KW ATP-binding; Chaperone; Coiled coil; Nucleotide-binding; Proteasome;
KW Reference proteome.
FT CHAIN 1..592
FT /note="Proteasome-associated ATPase"
FT /id="PRO_0000397008"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..592
FT /note="Docks into pockets in the proteasome alpha-ring"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT COILED 25..99
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 281..286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
SQ SEQUENCE 592 AA; 65654 MW; E9F00ADB98961251 CRC64;
MTGYDSSEEA ERDSSPADGY RQTPAQLSAQ IRVLNDEIAQ LRRRLAITPT DTRPLERQLT
ESANRINALS ERNEKLVVTL RDARAQLLQL KEEVDRLAQP PSGYGVFLSA GPEGTAEVFT
GGRRMRLAVS PTVEVEQLKR GQQLRLNEAL TVVEAAQFDV IGEVCSLREV LDGDRALVVG
HADEERVVHL AAPLMDIALK PGDSLLIDSK AGYAYERVPK SEVEDLVLEE VPDVAYEDIG
GLTRQIEQIR DAVELPFLHA DLYREYKLRP PKGVLLYGPP GCGKTLIAKA VANSLAKKVA
ALRGEETHTS YFLNIKGPEL LNKYVGETER TIRLIFQRAR EKASDGTPVI VFFDEMDSVF
RTRGTGVSSD VETTIVPQLL SEIDGVEGLE NVIVIGASNR EDMIDPAILR PGRLDVKIKI
ERPDAEAARD IFTKYLVTEL PIHPEDLAEF GGDRQACLSG MIQHTVERMY TETDENRFLE
VTYANGDKEV LYFKDFNSGA MIQNIVDRAK KSAIKSRIET GVNGLRVSQL LEAITDEFAE
NEDLPNTTNP DDWARISGKK GERIVYIRTL VSGKQSEGSR AIDTASNTGQ YL
