ARC_STRSW
ID ARC_STRSW Reviewed; 588 AA.
AC C9Z319;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 65.
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=SCAB_73441;
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=680198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22;
RX PubMed=20064060; DOI=10.1094/mpmi-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(2010).
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=CBG74328.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; FN554889; CBG74328.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_037725761.1; NC_013929.1.
DR AlphaFoldDB; C9Z319; -.
DR SMR; C9Z319; -.
DR STRING; 680198.SCAB_73441; -.
DR EnsemblBacteria; CBG74328; CBG74328; SCAB_73441.
DR GeneID; 24306444; -.
DR KEGG; scb:SCAB_73441; -.
DR eggNOG; COG1222; Bacteria.
DR HOGENOM; CLU_036054_0_0_11; -.
DR OrthoDB; 1115436at2; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000001444; 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..588
FT /note="Proteasome-associated ATPase"
FT /id="PRO_0000397025"
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; 65300 MW; D8CABE5C5A09BCA2 CRC64;
MAAHDDDMNR GIRPGRGSDD PSGQIAYLEQ EIAVLRRKLA DSPRHTRILE ERIVELQTNL
AGVSAQNERL ANTLREARDQ IVALKEEVDR LAQPPAGFGV FLTANEDGTA DIFTGGRKLR
VNVSPSVDLE ELRRGQEVML NEALNVVEAM EYESVGDIVT LKEILEDGER ALVQGHTDEE
RVVRLAEPLL DITIRPGDAL LLEPRSGYVY EVVPKSEVEE LVLEEVPDIG YEQIGGLGNQ
IEMIRDAVEL PYLYPDLFKE HELRPPKGVL LYGPPGCGKT LIAKAVANSL AKKVAEVTGQ
AQGKSFFLNI KGPELLNKYV GETERQIRLV FQRAREKASE GTPVIVFFDE MESLFRTRGS
GVSSDVENTI VPQLLAEIDG VEGLQNVVVI GASNREDMID PAILRPGRLD VKIKIERPDA
EAAKDIFQKY LTERLPLHTD DLGEHGGSKA TTVQSMIQTA VEHMYAESEE NRFLEVTYAN
GDKEVLYFKD FNSGAMIENI VGRAKKMAIK DFLDKNQKGL RVSHLLQACV DEFKENEDLP
NTTNPDDWAR ISGKKGERIV YIRTLITGKQ GADTGRSIDT VANTGQYL
