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ARC_RENSM
ID   ARC_RENSM               Reviewed;         594 AA.
AC   A9WSI4;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
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};
GN   OrderedLocusNames=RSal33209_2039;
OS   Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS   NBRC 15589 / NCIMB 2235).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Renibacterium.
OX   NCBI_TaxID=288705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235;
RX   PubMed=18723615; DOI=10.1128/jb.00721-08;
RA   Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA   Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA   Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT   "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT   reductive evolution away from an environmental Arthrobacter ancestor.";
RL   J. Bacteriol. 190:6970-6982(2008).
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; CP000910; ABY23772.1; -; Genomic_DNA.
DR   RefSeq; WP_012245442.1; NC_010168.1.
DR   AlphaFoldDB; A9WSI4; -.
DR   SMR; A9WSI4; -.
DR   STRING; 288705.RSal33209_2039; -.
DR   PRIDE; A9WSI4; -.
DR   EnsemblBacteria; ABY23772; ABY23772; RSal33209_2039.
DR   KEGG; rsa:RSal33209_2039; -.
DR   eggNOG; COG1222; Bacteria.
DR   HOGENOM; CLU_036054_0_0_11; -.
DR   OMA; CVDEFKE; -.
DR   OrthoDB; 1115436at2; -.
DR   UniPathway; UPA00997; -.
DR   Proteomes; UP000002007; 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..594
FT                   /note="Proteasome-associated ATPase"
FT                   /id="PRO_0000397011"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          593..594
FT                   /note="Docks into pockets in the proteasome alpha-ring"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT   COILED          18..71
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT   BINDING         282..287
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
SQ   SEQUENCE   594 AA;  65129 MW;  385FB676F6D4CFFD CRC64;
     MTETSANKPE NTQAHEGRDY SVLERQFNVL RDKLRNVDRQ LAAATQNNTK MTTTLQSAKA
     EILRLKSALE KDGQAPYSFA TLVQINPRRT PGQAVSTLSA ADQASSATGL AVTEESVDIA
     YQGRKMRVGL SPLVNIASLS PGQEVLLNES LTVIAGLGFE RTGEIVSVKE LIGTDRALVT
     GRADEERVVK LSGALMSQKI RVGDALSADS RSGYALEKVP RSEVENLILE EVPDISYHDI
     GGLGPQIEQI RDAVELPFLH PDLYREHGLK APKGILLYGP PGCGKTLIAK AVANSLAARA
     AERNGLKETK SFFLNIKGPE LLDKYVGETE RKIRLIFARA REKASDGSAV VVFFDEMDSL
     FRTRGTGVSS DVETTIVPQL LSEIDGVERL DNVIVIGASN REDMIDPAIL RPGRLDVKVK
     IQRPDAEAAA DIFAKYVTVD LPLHQDDLLA HGNSAQATVD AMIQRTVEAM YSTDKSNEYL
     EVTYANGDSE MLYFKDFNSG AVIQNVVDRA KKYAIKDLLT TGDKGIRVDH MLRAVADEFR
     EHEDMPNTTN PDDWARISDK KGERITYIRT IIQGKAGQEP GKTLETSLNT GQYL
 
 
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