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Database: UniProt
Entry: A0A1I2F4G5_9MICO
LinkDB: A0A1I2F4G5_9MICO
Original site: A0A1I2F4G5_9MICO 
ID   A0A1I2F4G5_9MICO        Unreviewed;       537 AA.
AC   A0A1I2F4G5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=SAMN04488035_1099 {ECO:0000313|EMBL:SFE99747.1};
OS   Flavimobilis marinus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Jonesiaceae;
OC   Flavimobilis.
OX   NCBI_TaxID=285351 {ECO:0000313|EMBL:SFE99747.1, ECO:0000313|Proteomes:UP000198520};
RN   [1] {ECO:0000313|Proteomes:UP000198520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19083 {ECO:0000313|Proteomes:UP000198520};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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.
CC       {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|HAMAP-Rule:MF_02112,
CC       ECO:0000256|RuleBase:RU003651}.
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DR   EMBL; FONZ01000002; SFE99747.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2F4G5; -.
DR   STRING; 285351.SAMN04488035_1099; -.
DR   OrthoDB; 9809379at2; -.
DR   Proteomes; UP000198520; 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: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|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}; Proteasome {ECO:0000313|EMBL:SFE99747.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198520}.
FT   DOMAIN          211..369
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   COILED          9..36
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
FT   BINDING         222..227
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
SQ   SEQUENCE   537 AA;  58054 MW;  022A247CA1ACF514 CRC64;
     MPDVTGEQVQ LLAARNERLV EALTAAREQI VTLKEQLDEL ARPPGGYGVF LAKVDASTAD
     VVSAGRKMHL AVAPDVDLDA LLPGQEVRLN EALVVVAAGG YEAVGELGVV REQLPDGRLL
     VVLRSDTEHV VRAAGRLAGV RVGDTVTVDA RAGFAFEEIE QSEVTDLVLE EVPDVDYADI
     GGLGAQIEQI RDAIELPIAH ADLFREHGLK APKGVLLYGP PGCGKTLIAK AVASSLSQML
     AARAGGETDG ARQRSYFLNI KGPELLNKYV GETERHIRTI FARAREKAAE GAPVVVFFDE
     MESLFRTRGT GVSSDVETTI VPQLLAEIDG VERLDNVIVI GASNREDMID PAILRPGRLD
     VKIKIERPDA EGARDIFAKY VLPDLPLHAD DLAEHGGDRA ATVAAMIDRT VERMYATDEA
     NAFLEVTYAS GDKEVLYFKD FASGAMIQNV VDRAKKHAVK DLLATGQRGL RVDHLLTACA
     AEFKENEDLP NTTNPDDWAR VSGKKGERIV FIRTIVQDAK QSSTARGIEP TATGQYL
//
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