ID A0A0L0JPI4_9ACTN Unreviewed; 588 AA.
AC A0A0L0JPI4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=IQ63_35080 {ECO:0000313|EMBL:KND27488.1};
OS Streptomyces acidiscabies.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=42234 {ECO:0000313|EMBL:KND27488.1, ECO:0000313|Proteomes:UP000037151};
RN [1] {ECO:0000313|Proteomes:UP000037151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 4445 {ECO:0000313|Proteomes:UP000037151};
RA Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT "Genome sequencing of plant-pathogenic Streptomyces species.";
RL Submitted (JUL-2014) 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:KND27488.1}.
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DR EMBL; JPPY01000195; KND27488.1; -; Genomic_DNA.
DR RefSeq; WP_050374418.1; NZ_KQ257832.1.
DR AlphaFoldDB; A0A0L0JPI4; -.
DR PATRIC; fig|42234.21.peg.7228; -.
DR OrthoDB; 9809379at2; -.
DR Proteomes; UP000037151; Unassembled WGS sequence.
DR GO; GO:0000502; C:proteasome complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:InterPro.
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; IPR018177; L-lactate_DH_AS.
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.
DR PROSITE; PS00064; L_LDH; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000037151}.
FT DOMAIN 265..419
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 53..94
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 588 AA; 65109 MW; 838B8CBA612921B7 CRC64;
MAAHDDDMNR GIRPGRGSDD PSGQIAYLEQ EIAVLRRKLA DSPRHTRILE ERIVELQTNL
AGVSAQNERL ANTLREARDQ IVALKEEVDR LAQPPAGFGV FLTANEDGTA DIFTGGRKLR
VNVSPSVDLD ALRRGQEVML NEALNVVEAM EYESVGDIVT LKEILEDGER ALVQGHTDEE
RVVRLAEPLL DVTIRPGDAL LLEPRSGYVY EIVPKSEVEE LVLEEVPDIG YEQIGGLGGQ
IEAIRDAVEL PYLYPDLFKE HELRPPKGVL LYGPPGCGKT LIAKAVANSL AKKVAEVTGQ
AQGKSFFLNI KGPELLNKYV GETERQIRLV FQRAREKASE GTPVIVFFDE MESLFRTRGS
GVSSDVENTI VPQLLAEIDG VEGLQNVVVI GASNREDMID PAILRPGRLD VKIKIERPDA
EAAKDIFGKY LTERLPLHPD DVGEHGDSKT VTVDSMIQTA VEHMYAESEE NRFLEVTYAN
GDKEVLYFKD FNSGAMIENI VGRAKKMAIK DFLDQKQKGI RVSHLLQACV DEFKENEDLP
NTTNPDDWAR ISGKKGERIV YIRTLITGKQ GADTGRSIDT VANTGQYL
//
