ID I7L942_9CORY Unreviewed; 532 AA.
AC I7L942;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 10-JUN-2026, entry version 75.
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=HMPREF9719_00651 {ECO:0000313|EMBL:EJZ82426.1};
OS Corynebacterium otitidis ATCC 51513.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=883169 {ECO:0000313|EMBL:EJZ82426.1, ECO:0000313|Proteomes:UP000006078};
RN [1] {ECO:0000313|EMBL:EJZ82426.1, ECO:0000313|Proteomes:UP000006078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51513 {ECO:0000313|EMBL:EJZ82426.1,
RC ECO:0000313|Proteomes:UP000006078};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Turicella otitidis ATCC 51513.";
RL Submitted (AUG-2012) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJZ82426.1}.
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DR EMBL; AHAE01000032; EJZ82426.1; -; Genomic_DNA.
DR RefSeq; WP_004600541.1; NZ_HF541866.1.
DR STRING; 29321.AAV33_00335; -.
DR PATRIC; fig|883169.3.peg.623; -.
DR eggNOG; COG1222; Bacteria.
DR HOGENOM; CLU_036054_0_0_11; -.
DR OrthoDB; 9809379at2; -.
DR Proteomes; UP000006078; Unassembled WGS sequence.
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 FunFam; 3.40.50.300:FF:001025; ATPase family, AAA domain-containing 2B; 1.
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; IPR050168; AAA_ATPase_domain.
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:SF144; PROTEASOME-ASSOCIATED ATPASE; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02112};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_02112};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02112}; Proteasome {ECO:0000313|EMBL:EJZ82426.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006078}.
FT DOMAIN 235..396
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 35..62
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
FT COMPBIAS 7..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 246..251
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
SQ SEQUENCE 532 AA; 57384 MW; E10DEF18074CD291 CRC64;
MTLSRPDTGH TGRDEGDRRF HGDLLRENRT LSARNKKLAE LLKASRDKLD TLRQQIEDLN
QPPSTYGTFL ERSEDGEHAE IVALGRQMRV PVSPAVSFGE LEAGTLVRLG EGSQVLEACG
PSPTGEVAAI KEVLDDRRAV VVDSAGDARV VRLSRAVREA ARGPRPGDEV LVEPKAGVAV
ELLPVTDVAQ LSLEEVPEVS YEDIGGLDEQ IATIHDAVEL PFLHPELFRS YDLKPPKGVL
LYGPPGCGKT LIAKAVAHSL ASKTLRGDCP CLDTEAPESP RAYFLNIKGP ELLNKYVGET
ERQVRAIFER ARELAADGSA VVVFFDEMES LFRTRGSGKS SDVETTVVPQ LLTELDGVEQ
LENVIVIGAT NREELIDPAL MRPGRLDVKI PVARPDRKAG ADIFARYLSG GIPLAGPAAE
LVDAGVAVLY EKRPVLEVEF VDGSSRAMTA DEFVSGAMIA SVVDRAKKIA VKDELSGGRP
GITAEHVRAA ARQEAAENEA LAGGEDPSAW LHISGLKGKK VRFVRRIGRE GS
//
