ID   ARC_MYCBT               Reviewed;         609 AA.
AC   C1AQ31;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=Mycobacterial proteasome ATPase {ECO:0000255|HAMAP-Rule:MF_02112};
GN   Name=mpa {ECO:0000255|HAMAP-Rule:MF_02112}; OrderedLocusNames=JTY_2126;
OS   Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=561275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Tokyo 172 / ATCC 35737 / TMC 1019;
RX   PubMed=19200449; DOI=10.1016/j.vaccine.2009.01.034;
RA   Seki M., Honda I., Fujita I., Yano I., Yamamoto S., Koyama A.;
RT   "Whole genome sequence analysis of Mycobacterium bovis bacillus Calmette-
RT   Guerin (BCG) Tokyo 172: a comparative study of BCG vaccine substrains.";
RL   Vaccine 27:1710-1716(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}.
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; AP010918; BAH26410.1; -; Genomic_DNA.
DR   RefSeq; WP_003411035.1; NZ_CP014566.1.
DR   AlphaFoldDB; C1AQ31; -.
DR   SMR; C1AQ31; -.
DR   KEGG; mbt:JTY_2126; -.
DR   HOGENOM; CLU_036054_0_0_11; -.
DR   OMA; CVDEFKE; -.
DR   UniPathway; UPA00997; -.
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.
FT   CHAIN           1..609
FT                   /note="Proteasome-associated ATPase"
FT                   /id="PRO_0000396995"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          608..609
FT                   /note="Docks into pockets in the proteasome alpha-ring"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT   COILED          20..96
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT   BINDING         296..301
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
SQ   SEQUENCE   609 AA;  67401 MW;  4D5F4E630614C58D CRC64;
     MGESERSEAF GIPRDSPLSS GDAAELEQLR REAAVLREQL ENAVGSHAPT RSARDIHQLE
     ARIDSLAARN SKLMETLKEA RQQLLALREE VDRLGQPPSG YGVLLATHDD DTVDVFTSGR
     KMRLTCSPNI DAASLKKGQT VRLNEALTVV EAGTFEAVGE ISTLREILAD GHRALVVGHA
     DEERVVWLAD PLIAEDLPDG LPEALNDDTR PRKLRPGDSL LVDTKAGYAF ERIPKAEVED
     LVLEEVPDVS YADIGGLSRQ IEQIRDAVEL PFLHKELYRE YSLRPPKGVL LYGPPGCGKT
     LIAKAVANSL AKKMAEVRGD DAHEAKSYFL NIKGPELLNK FVGETERHIR LIFQRAREKA
     SEGTPVIVFF DEMDSIFRTR GTGVSSDVET TVVPQLLSEI DGVEGLENVI VIGASNREDM
     IDPAILRPGR LDVKIKIERP DAEAAQDIYS KYLTEFLPVH ADDLAEFDGD RSACIKAMIE
     KVVDRMYAEI DDNRFLEVTY ANGDKEVMYF KDFNSGAMIQ NVVDRAKKNA IKSVLETGQP
     GLRIQHLLDS IVDEFAENED LPNTTNPDDW ARISGKKGER IVYIRTLVTG KSSSASRAID
     TESNLGQYL