ID   ARC_STRCO               Reviewed;         588 AA.
AC   Q9RJ58; O87594;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 123.
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=SCO1648;
GN   ORFNames=SCI41.31c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=9765579; DOI=10.1128/jb.180.20.5448-5453.1998;
RA   Nagy I., Tamura T., Vanderleyden J., Baumeister W., De Mot R.;
RT   "The 20S proteasome of Streptomyces coelicolor.";
RL   J. Bacteriol. 180:5448-5453(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC64282.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF086832; AAC64282.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL939109; CAB59501.1; -; Genomic_DNA.
DR   RefSeq; NP_625923.1; NC_003888.3.
DR   RefSeq; WP_011027900.1; NZ_VNID01000018.1.
DR   AlphaFoldDB; Q9RJ58; -.
DR   SMR; Q9RJ58; -.
DR   STRING; 100226.SCO1648; -.
DR   GeneID; 1097079; -.
DR   KEGG; sco:SCO1648; -.
DR   PATRIC; fig|100226.15.peg.1662; -.
DR   eggNOG; COG1222; Bacteria.
DR   HOGENOM; CLU_036054_0_0_11; -.
DR   InParanoid; Q9RJ58; -.
DR   OMA; CVDEFKE; -.
DR   PhylomeDB; Q9RJ58; -.
DR   UniPathway; UPA00997; -.
DR   Proteomes; UP000001973; 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; IBA:GO_Central.
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..588
FT                   /note="Proteasome-associated ATPase"
FT                   /id="PRO_0000397023"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          587..588
FT                   /note="Docks into pockets in the proteasome alpha-ring"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT   COILED          47..94
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT   BINDING         276..281
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
SQ   SEQUENCE   588 AA;  65174 MW;  B9B44F2A1FBCF0B8 CRC64;
     MAAHDDDMNR GIRPGRGSED PAGQVAYLEQ EIAVLRRKLA ESPRHTRILE ERIVELQTNL
     AGVSAQNERL AGTLREARDQ IVALKEEVDR LAQPPAGFGV FLQANEDGTA DIFTGGRKLR
     VNVSPSVELD ELRRGQEVML NEALNVVEAM EYESVGDIVT LKEILEDGER ALVLGHTDEE
     RVVRLAEPLR GLTIRPGDAL LLEPRSGYVY EVVPKSEVEE LVLEEVPDIG YEQIGGLGGQ
     IEMIRDAVEL PYLYPDLFRE HELRPPKGVL LYGPPGCGKT LIAKAVANSL AKKVAEVTGQ
     AAGKSFFLNI KGPELLNKYV GETERQIRLV FQRAREKASE GTPVIVFFDE MESLFRTRGS
     GVSSDVENTI VPQLLAEIDG VEGLQNVVVI GASNREDMID PAILRPGRLD VKIKIERPDA
     EAAKDIFGKY LTERLPLHSD DLAEHEKDKS ATVSSMIQTA VEQMYAESEE NRFLEVTYAN
     GDKEVLYFKD FNSGAMIENI VGRAKKMAIK DFLDKNQKGL RVSHLLQACV DEFKENEDLP
     NTTNPDDWAR ISGKKGERIV YIRTLVTGKQ GADTGRSIDT VANTGQYL