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Database: UniProt
Entry: A0A1A3C1U4_9MYCO
LinkDB: A0A1A3C1U4_9MYCO
Original site: A0A1A3C1U4_9MYCO 
ID   A0A1A3C1U4_9MYCO        Unreviewed;       613 AA.
AC   A0A1A3C1U4;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 41.
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=A5663_17420 {ECO:0000313|EMBL:OBI80598.1};
OS   Mycobacterium sp. E740.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1834149 {ECO:0000313|EMBL:OBI80598.1, ECO:0000313|Proteomes:UP000092151};
RN   [1] {ECO:0000313|Proteomes:UP000092151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E740 {ECO:0000313|Proteomes:UP000092151};
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Sam S., Sreng N.,
RA   Him V., Kerleguer A., Cheng S.;
RL   Submitted (JUN-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}.
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:OBI80598.1}.
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DR   EMBL; LZKP01000087; OBI80598.1; -; Genomic_DNA.
DR   RefSeq; WP_068146471.1; NZ_LZKP01000087.1.
DR   AlphaFoldDB; A0A1A3C1U4; -.
DR   STRING; 1834149.A5663_17420; -.
DR   OrthoDB; 9809379at2; -.
DR   Proteomes; UP000092151; 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}; Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02112,
KW   ECO:0000256|RuleBase:RU003651};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000313|EMBL:OBI80598.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092151}.
FT   DOMAIN          289..445
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         300..305
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
SQ   SEQUENCE   613 AA;  68128 MW;  1B6D734CA39CC0FD CRC64;
     MSESERSEAY SEGLGAPHES GMSSEDAAEL EELRREAAVL REQLENAVGP QSGLRSARDV
     HQLEARIDSL AARNAKLMET LKEARQQLLA LREEVDRLGQ PPSGYGVLLG VQEDDTVDVF
     TSGRKMRLTC SPNIDAKALK QGQTVRLNEA LTVVEAGNFE AVGEISTLRE ILSDGHRALV
     VGHADEERIV WLAEPLVAAE HLPDDYDDDL DDGRPRKLRP GDSLLVDTKA GYAFERIPKA
     EVEDLVLEEV PDVSYNDIGG LGRQIEQIRD AVELPFLHKE LYREYSLRPP KGVLLYGPPG
     CGKTLIAKAV ANSLAKKMAE VRGDDAREAK SYFLNIKGPE LLNKFVGETE RHIRLIFQRA
     REKASEGTPV IVFFDEMDSI FRTRGTGVSS DVETTVVPQL LSEIDGVEGL ENVIVIGASN
     REDMIDPAIL RPGRLDVKIK IERPDAEAAQ DIFSKYLTEE LPVNEDDLTE FGGDRSLTIK
     AMIEKVVDRM YAEIDDNRFL EVTYANGDKE VMYFKDFNSG AMIQNVVDRA KKYAIKSVLE
     TGKRGLRIQH LLDSIVDEFA ENEDLPNTTN PDDWARISGK KGERIVYIRT LVTGKTSSAS
     RAIDTESNLG QYL
//
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