ID A0A1H2M5P4_9ACTN Unreviewed; 587 AA.
AC A0A1H2M5P4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=AAA ATPase forming ring-shaped complexes {ECO:0000256|HAMAP-Rule:MF_02112};
DE Short=ARC {ECO:0000256|HAMAP-Rule:MF_02112};
GN Name=arc {ECO:0000256|HAMAP-Rule:MF_02112};
GN ORFNames=SAMN04488544_1452 {ECO:0000313|EMBL:SDU88573.1};
OS Microlunatus sagamiharensis.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Microlunatus.
OX NCBI_TaxID=546874 {ECO:0000313|EMBL:SDU88573.1, ECO:0000313|Proteomes:UP000198825};
RN [1] {ECO:0000313|Proteomes:UP000198825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21743 {ECO:0000313|Proteomes:UP000198825};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer. Assembles into a hexameric ring structure.
CC {ECO:0000256|HAMAP-Rule:MF_02112}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000256|HAMAP-
CC Rule:MF_02112, ECO:0000256|RuleBase:RU003651}.
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DR EMBL; LT629799; SDU88573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2M5P4; -.
DR STRING; 546874.SAMN04488544_1452; -.
DR OrthoDB; 9809379at2; -.
DR Proteomes; UP000198825; Chromosome i.
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; 1.10.8.60; -; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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_2nd.
DR InterPro; IPR041626; Prot_ATP_ID_OB_N.
DR InterPro; IPR022482; Proteasome_ATPase.
DR NCBIfam; TIGR03689; pup_AAA; 1.
DR PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR PANTHER; PTHR23077:SF171; ATPASE FAMILY PROTEIN 2 HOMOLOG; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR Pfam; PF17758; Prot_ATP_ID_OB_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02112,
KW ECO:0000256|RuleBase:RU003651};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_02112};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02112,
KW ECO:0000256|RuleBase:RU003651}; Proteasome {ECO:0000313|EMBL:SDU88573.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198825}.
FT DOMAIN 265..418
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 18..87
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
FT BINDING 276..281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
SQ SEQUENCE 587 AA; 64852 MW; 323B836D404EAB7E CRC64;
MSGSSYGSGL GGSSYEDRES LLVQIGALRE ELARLRERVS AHPHDLAVLE RRLTDARAEA
RTTTANNERL AATLREARDQ IVTLKGEVDR LAQPPASFGV FIAAAEDRTA DIFTSGRKMR
VSVSPDVDLE ALEPGREVMV NEAMNVVRAL DFDEVGEIAT LKEVLEGGER ALVVGHGDEE
SVVRLATRLQ EGPIRAGDSL LIDRRVHFAY ERVPKLEVEE LVLEEVPDID YSVIGGLGGQ
IEAIRDAVEL PFLHKDLFAE HQLKAPKGIL LYGPPGCGKT LIAKAVANSL AKRVTEKTGV
EGRSFFLNIK GPELLNKYVG ETERHIRLVF QRAREKASDG MPVIVFFDEM DSLFRTRGTG
VSSDVENTIV PQLLSEIDGV EGLENVIIIG ASNREDMIDP AILRPGRLDV KIKIERPDAE
AARDIFSKYL LPSLPLHTED LDEFAGDAER TVRGMIERTV ERMYTDTEEN QFLEVTYAGG
DKEILYFRDF NSGAMVQNIV DRAKKMAIKD LLDTGVKGIR IGHLLQACVD EFAENEDLPN
TTNPDDWAKI SGKKGERIVF IRTLISSKKG TQAGRSIDTV TNTGQYL
//