ARC_FRAAA
ID ARC_FRAAA Reviewed; 601 AA.
AC Q0RLU1;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
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}; OrderedLocusNames=FRAAL2869;
OS Frankia alni (strain ACN14a).
OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=326424;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACN14a;
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
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=CAJ61513.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CT573213; CAJ61513.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041939236.1; NC_008278.1.
DR AlphaFoldDB; Q0RLU1; -.
DR SMR; Q0RLU1; -.
DR STRING; 326424.FRAAL2869; -.
DR KEGG; fal:FRAAL2869; -.
DR eggNOG; COG1222; Bacteria.
DR HOGENOM; CLU_036054_0_0_11; -.
DR OrthoDB; 1115436at2; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000000657; 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..601
FT /note="Proteasome-associated ATPase"
FT /id="PRO_0000396982"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..601
FT /note="Docks into pockets in the proteasome alpha-ring"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT COILED 18..106
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 289..294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
SQ SEQUENCE 601 AA; 66490 MW; 6125DBCF5A839F34 CRC64;
MSGPRSGSGS GGSTGRPGDA ESRRSAYEKE AHELTTQVAF LEEEVAMLRR RLSESPRQVR
VLEERLAEVQ AELSSATGQN DRLVATLREA RDQIVTLKEE VDRLAQPPSG YGIFVSRYDD
GTVDVFTQGR KLRVTVSPSV DVGSLSPGQE VMLNEALNVV EARSFERQGE IVLLKEVLES
GDRALVIGHT DEERVVMLAQ PLLDGPIRAG DSLLIEPRSG YAFERVPKSE VEELVLEEVP
DIGYEQIGGL KSQIESIRDS VELPFLYKDL YREHQLKPPK GVLLYGPPGC GKTLIAKAVA
NSLAKKVEAI TGQGNGRAFF LNIKGPELLN KFVGETERQI RLVFQRAREK ASEGMPVIVF
FDEMDSIFRT RGSGVSSDVE NTIVPQLLSE IDGVEQLENV IVIGASNRED MIDPAILRPG
RLDVKIKVER PDAEAARDIF AKYVVPSLPL YPEDLAEFDG NREATVAAMI QRVVERMYAE
SEENRFLEVT YANGDKEVLY FKDFNSGAMI ENIVARAKKM AVKAHIEGGL KGLRMQYLLA
ACLDEFKENE DLPNTTNPDD WARISGKKGE RIVYIRTLVT GTKGTEAGRS IDTIANTGQY
L
