ARC_MYCA9
ID ARC_MYCA9 Reviewed; 602 AA.
AC B1MAH2;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=MAB_2162;
OS Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM
OS 13569 / NCTC 13031 / TMC 1543) (Mycobacterium abscessus).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacteroides; Mycobacteroides abscessus.
OX NCBI_TaxID=561007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC
RC 1543;
RX PubMed=19543527; DOI=10.1371/journal.pone.0005660;
RA Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M.,
RA Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L.,
RA Gaillard J.L.;
RT "Non mycobacterial virulence genes in the genome of the emerging pathogen
RT Mycobacterium abscessus.";
RL PLoS ONE 4:E5660-E5660(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; CU458896; CAM62243.1; -; Genomic_DNA.
DR RefSeq; WP_005086527.1; NZ_MLCG01000002.1.
DR AlphaFoldDB; B1MAH2; -.
DR SMR; B1MAH2; -.
DR EnsemblBacteria; CAM62243; CAM62243; MAB_2162.
DR GeneID; 66972533; -.
DR KEGG; mab:MAB_2162; -.
DR OMA; CVDEFKE; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000007137; 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.
FT CHAIN 1..602
FT /note="Proteasome-associated ATPase"
FT /id="PRO_0000396992"
FT REGION 601..602
FT /note="Docks into pockets in the proteasome alpha-ring"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT COILED 13..89
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT BINDING 289..294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
SQ SEQUENCE 602 AA; 66656 MW; 492D17D1BB04ED7F CRC64;
MSESERSEAF GTPDAAEVER LRREVAALRE QLEGSAARGP GDSGRLRDLN QLEARIDSLN
ARNAKLMDTL KEARQQLLAL REEVDRLGQP PSGYGVLLAV QTDETVDVFT SGRKMRVTCS
PNIETSELRR GQTVRLNEAL TVVEAGNFES VGEISTLREV LDDGHRALVV GHADEERIVW
LADPLIAPDL SEVSEDADGA DLKPRKLRPG DSLLVDTKAG YAFERIPKAE VEDLVLEEVP
DVSYSDIGGL ARQIEQIRDA VELPFLHKDL YQEYSLRPPK GVLLYGPPGC GKTLIAKAVA
NSLAKKMAEL RGDDSREAKS YFLNIKGPEL LNKFVGETER HIRLIFQRAR EKASDGTPVI
VFFDEMDSIF RTRGTGVSSD VETTVVPQLL SEIDGVEGLE NVIVIGASNR EDMIDPAILR
PGRLDVKIKI ERPDAESAQD IFSKYLTVDL PVHSEDLAEF GGDRGLTVKA MIEKVVDRMY
AEIDDNRFLE VTYANGDKEV MYFKDFNSGA MIQNVVDRAK KNAIKSVLET GQKGLRIQHL
LDSIVDEFAE NEDLPNTTNP DDWARISGKK GERIVYIRTL VTGKSSSASR AIDTESSLGQ
YL
