ARC_THECD
ID ARC_THECD Reviewed; 587 AA.
AC D1A2S5;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=Tcur_2307;
OS Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC Bacteria; Actinobacteria; Streptosporangiales; Thermomonosporaceae;
OC Thermomonospora.
OX NCBI_TaxID=471852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 / NCIMB
RC 10081 / Henssen B9;
RX PubMed=21475583; DOI=10.4056/sigs.1453580;
RA Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brettin T., Han C., Detter J.C., Rohde M., Goeker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL Stand. Genomic Sci. 1:13-22(2011).
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; CP001738; ACY97873.1; -; Genomic_DNA.
DR RefSeq; WP_012852657.1; NC_013510.1.
DR AlphaFoldDB; D1A2S5; -.
DR SMR; D1A2S5; -.
DR STRING; 471852.Tcur_2307; -.
DR EnsemblBacteria; ACY97873; ACY97873; Tcur_2307.
DR KEGG; tcu:Tcur_2307; -.
DR eggNOG; COG1222; Bacteria.
DR HOGENOM; CLU_036054_0_0_11; -.
DR OMA; CVDEFKE; -.
DR OrthoDB; 1115436at2; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000001918; 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..587
FT /note="Proteasome-associated ATPase"
FT /id="PRO_0000397028"
FT REGION 586..587
FT /note="Docks into pockets in the proteasome alpha-ring"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT COILED 9..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 587 AA; 65001 MW; E5DAF8ACB9121D43 CRC64;
MAARDDAGAR KAQHDAEIHD LRSQVSMLEE EVSVLRRKLA ESPRQIRVLE DRLHETQAKL
AAVTGQNERL VATLKEAREQ IIALKEEVDR LAQPPSGFGV FLGAREDGTV DIFTGGRKLR
VNVSPSVDVS QLKQGQEVLL NEALNVVEAL GYETQGEVVM LKELFDDGER ALVIAHADEE
RVIKLAEPLR GVPLRAGDSL MLEPRSGYAY EKIHKAEVEE LVLEEVPDIT YEEIGGLGPQ
IEQIRDAVEL PYLHADLFRE HKLRPPKGVL LYGPPGCGKT LIAKAVANSL AKQVAEKTGQ
EGKSFFLNIK GPELLNKYVG ETERHIRLVF QRAREKASAG TPVIVFFDEM DSIFRTRGSG
VSSDVENTIV PQLLSEIDGV EGLENVIVIG ASNREDMIDP AILRPGRLDV KIKIERPDAE
AAKDIFSKYL VPGLPLHPDD LAEHGGSEEA TIEAMIQRVV ERMYAETEEN RFLEVTYANG
DKEVLYFKDF NSGAMIQNIV DRAKKMAIKQ YLETGQKGLR VSHLLAACVD EFSENEDLPN
TTNPDDWARI SGKKGERIVY IRTLVSGKAG SEAGRSIDTV ANTGQYL
