ID   ARC_NOCFA               Reviewed;         586 AA.
AC   Q5YUW4;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=NFA_31800;
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=247156;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152;
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AP006618; BAD58027.1; -; Genomic_DNA.
DR   RefSeq; WP_011209712.1; NC_006361.1.
DR   AlphaFoldDB; Q5YUW4; -.
DR   SMR; Q5YUW4; -.
DR   STRING; 247156.NFA_31800; -.
DR   EnsemblBacteria; BAD58027; BAD58027; NFA_31800.
DR   GeneID; 61133895; -.
DR   KEGG; nfa:NFA_31800; -.
DR   eggNOG; COG1222; Bacteria.
DR   HOGENOM; CLU_036054_0_0_11; -.
DR   OMA; CVDEFKE; -.
DR   UniPathway; UPA00997; -.
DR   Proteomes; UP000006820; 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..586
FT                   /note="Proteasome-associated ATPase"
FT                   /id="PRO_0000397009"
FT   REGION          585..586
FT                   /note="Docks into pockets in the proteasome alpha-ring"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT   COILED          11..76
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT   BINDING         273..278
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
SQ   SEQUENCE   586 AA;  65133 MW;  006875DFA434A085 CRC64;
     MSPIENSDSA AWRELEAVRA EAAALRRQLA DSPDRTRELE ARIDSLTIRN TKLMDTLKEA
     RQQLVALREE VDRLGQPPSG YGILIGVYDD QTVDVFTSGR KMRLTCSPNI DTSTLSYGQT
     VRLNEALTVV EANEYDAVGE IGTLREILDD GRRALVVGHA DEERVVWLAG PLAKVAEEDD
     LDDPDSPVRK LRPGDSLLVD TKAGFAFERI PKAEVEDLVL EEVPDVDYSD IGGLGRQIEQ
     IRDAVELPFL HKDLFREYEL RPPKGVLLYG PPGCGKTLIA KAVANSLAKK IAEARGEDAK
     EAKSFFLNIK GPELLNKFVG ETERHIRIIF QRAREKASEG TPVIVFFDEM DSIFRTRGSG
     VSSDVETTVV PQLLSEIDGV EGLENVIVIG ASNREDMIDP AILRPGRLDV KIKIERPDAE
     SAQDIFSKYL TEDLPLHADD LAEFGGDKAA CVRAMIERVV DRMYAESEDN RFLEVTYANG
     DKEVLYFKDF NSGAMIQNIV DRAKKYAIKS VLETGSPGLR IQHLYDSIVD EFSENEDLPN
     TTNPDDWARI SGKKGERIVY IRTLVTGKNA SASRAIDTES NTGQYL