ID A0A060JE88_9MICO Unreviewed; 714 AA.
AC A0A060JE88;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=ATPases with chaperone activity, ATP-binding subunit {ECO:0000313|EMBL:AIC48146.1};
GN ORFNames=Rhola_00013570 {ECO:0000313|EMBL:AIC48146.1};
OS Rhodoluna lacicola.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Luna cluster; Luna-1 subcluster; Rhodoluna.
OX NCBI_TaxID=529884 {ECO:0000313|EMBL:AIC48146.1, ECO:0000313|Proteomes:UP000067708};
RN [1] {ECO:0000313|EMBL:AIC48146.1, ECO:0000313|Proteomes:UP000067708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWH-Ta8 {ECO:0000313|EMBL:AIC48146.1,
RC ECO:0000313|Proteomes:UP000067708};
RX PubMed=24984700; DOI=10.1099/ijs.0.065292-0;
RA Hahn M., Schmidt J., Taipale S.J., Doolittle W.F., Koll U.;
RT "Rhodoluna lacicola gen. nov., sp. nov., a planktonic freshwater bacterium
RT with stream-lined genome.";
RL Int. J. Syst. Evol. Microbiol. 64:3254-3263(2014).
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP007490; AIC48146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060JE88; -.
DR STRING; 529884.Rhola_00013570; -.
DR KEGG; rla:Rhola_00013570; -.
DR PATRIC; fig|529884.3.peg.1314; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_11; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000067708; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000067708}.
FT DOMAIN 52..192
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 451..600
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 618..707
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT COILED 258..345
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 714 AA; 79067 MW; 581F05E87A627646 CRC64;
MNQPNMQQEE QKSALEQFGV NLTEIAKSGK LDPVIGRDAE IRRVSQVLSR RTKNNPVLIG
EPGVGKTAVV EGLAQRIVAG DVPESLKGKQ LISLDLAAMV AGAKYRGEFE ERLKAVLAEI
NASEGGIITF IDELHTLVGA GAADGQDASN MLKPMLARGE LRLIGATTLD EFRERIEKDP
ALERRFQQVY VGEPSVVDTI AILRGLKERY EAHHKVAIAD AALVAAATLS NRYIPSRQLP
DKAIDLIDEA ASRLRMEIDS APIEIDELRR QVDRLKLEEL ALKKEKDDAS KERLEKLRED
LADKSKRLDE LNERWAKERA ELNKVGELKT KLDGLRIEAE RAQREGNLER ASKLLYGDIP
ALEKELVATE TAESENTDRM VNDQVGEDDI AAVVSAWTGI PTGRLLAGES QKLLNLEAEL
GKRLIGQKVA VKSVSDAVRR TKAGISDPSR PTGSFMFLGP TGVGKTELAK SLAEFLFDDE
KAMVRIDMSE YGEKHSVSRL LGAPPGYIGY EEGGQLTEAV RRRPYSVVLL DEVEKAHPEV
FDVLLQVLDD GRLTDGQGRV VDFKNVILIM TSNLGSQFLI DQELTAEQKR DGVMTMVRAH
FKPEFLNRLD DIVIFTALDR SELGQIVELN IDRLAHRLEQ RRLQLAVTPA ARAWLADKGY
DPIYGARPLR RLMQQQIDDK LANLLLAGDI HDGSFVKVDV SEDGVQLEVS PGDI
//
