ID A0A1Q2HWM2_9CORY Unreviewed; 513 AA.
AC A0A1Q2HWM2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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=mpa {ECO:0000313|EMBL:AQQ15245.1};
GN Synonyms=arc {ECO:0000256|HAMAP-Rule:MF_02112};
GN ORFNames=CGLAU_06410 {ECO:0000313|EMBL:AQQ15245.1};
OS Corynebacterium glaucum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=187491 {ECO:0000313|EMBL:AQQ15245.1, ECO:0000313|Proteomes:UP000217209};
RN [1] {ECO:0000313|EMBL:AQQ15245.1, ECO:0000313|Proteomes:UP000217209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 30827 {ECO:0000313|EMBL:AQQ15245.1,
RC ECO:0000313|Proteomes:UP000217209};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-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; CP019688; AQQ15245.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2HWM2; -.
DR KEGG; cgv:CGLAU_06410; -.
DR OrthoDB; 9809379at2; -.
DR Proteomes; UP000217209; 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; 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};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02112,
KW ECO:0000256|RuleBase:RU003651}; Proteasome {ECO:0000313|EMBL:AQQ15245.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000217209}.
FT DOMAIN 222..371
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 233..238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
SQ SEQUENCE 513 AA; 56267 MW; CF688D513BF0CECB CRC64;
MIEDDAFGPE LRELKRENRA MSERNTKLAE LLKSSRDKLN LLYAQVEALG EPASTYGIFL
EDSPRGMEAE VFTSGRRMRV KVAPTVEPTS LAPGTLVRLG DGTVIVEACG YESTGQLAML
VEKIDGNRAV VADQQGTEHL VHLTDPLQEA ARAGDTMLID PKAGYAFERI PKTEVNQLSL
EEVPDVTYAD IGGLSSQIET IKDSVELPFA YPELYRQYRL APPKGLLLYG PPGCGKTLIA
KAVANSLSQR IGDGGQAHFI NVKGPELLNK FVGETERRIR LIFERARELA SDGRPVIVFF
DEMESIFRTR GSGVSSDMET TVVPQLLTEI DGVEDIANVI VIGATNREEL IDPAILRPGR
LDIKIRVSRP NREEAADIFA RYITADIPLA DSPETLIEAA VEELFAPRPF VRLQLVDGTF
ETLHYHDFVS GAMIANVVDR AKKLAIKDHI AGTNATGVTA AHLREAVRTE QDESEDMPNT
ANPDEWARIS GRQGKRIVAA EVLAGEKPRT ASV
//