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Database: UniProt
Entry: E0DEW4_9CORY
LinkDB: E0DEW4_9CORY
Original site: E0DEW4_9CORY 
ID   E0DEW4_9CORY            Unreviewed;       507 AA.
AC   E0DEW4;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 72.
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   ECO:0000313|EMBL:EFM49104.1};
GN   ORFNames=HMPREF0299_6400 {ECO:0000313|EMBL:EFM49104.1};
OS   Corynebacterium matruchotii ATCC 14266.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=553207 {ECO:0000313|EMBL:EFM49104.1, ECO:0000313|Proteomes:UP000004218};
RN   [1] {ECO:0000313|EMBL:EFM49104.1, ECO:0000313|Proteomes:UP000004218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14266 {ECO:0000313|EMBL:EFM49104.1,
RC   ECO:0000313|Proteomes:UP000004218};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (AUG-2010) 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:EFM49104.1}.
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DR   EMBL; ACSH02000005; EFM49104.1; -; Genomic_DNA.
DR   RefSeq; WP_005521171.1; NZ_ACSH02000005.1.
DR   AlphaFoldDB; E0DEW4; -.
DR   STRING; 553207.HMPREF0299_6400; -.
DR   GeneID; 84573875; -.
DR   eggNOG; COG1222; Bacteria.
DR   OrthoDB; 9809379at2; -.
DR   Proteomes; UP000004218; 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   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}; Hydrolase {ECO:0000313|EMBL:EFM49104.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02112,
KW   ECO:0000256|RuleBase:RU003651}; Proteasome {ECO:0000313|EMBL:EFM49104.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004218}.
FT   DOMAIN          224..373
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   COILED          9..44
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
FT   BINDING         235..240
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
SQ   SEQUENCE   507 AA;  55970 MW;  D2C35F7D7725DB0C CRC64;
     MHSSDIAWIK KTNDELKTRN AKLAELLKAS RDKLQVLHQQ LEELAAPPST YGTYLEPSPN
     GKTAEVFTAG RLMRLAISPL INPDDLVPGI QVRLGEAHEI VEACSYTTTG KLAILVEMID
     PTRALIVDQQ GEEHVARLAH PLANPTNPIN RRPRAGDTVL VDLKAGYVFE IIPKTEVARL
     VLEETPDATY ADIGGLDTQI EQIHDAVELP FTHPQLYRDY QLHPPKGVLL YGPPGCGKTL
     IAKAVANSLA SRVGDGESSY FINVKGPELL NKYVGETERR IRLIFERARE LAEAGRPVII
     FFDEMDSIFR TRGSGVSSDM ETTVVPQLLT ELDGVESLSN VIVIGATNRE ELIDPAVLRP
     GRLDVKIRVG RPTKDNAKEI FARHLDQSVP TADSVDKLIE VACEYMYADR PYVELTLVTG
     EVETLHYRDF ISGAMIANIV DRAKKSAIKA HLAGDPRGIT ADQLRQAIDA ENRESEDMPN
     TANPDEWSRI THRTGIRVAH ARVIGGN
//
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