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Database: UniProt
Entry: S9SC60_9RHOB
LinkDB: S9SC60_9RHOB
Original site: S9SC60_9RHOB 
ID   S9SC60_9RHOB            Unreviewed;       959 AA.
AC   S9SC60;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=ATPase with chaperone activity, ATP-binding subunit {ECO:0000313|EMBL:EPX87700.1};
GN   ORFNames=ruthe_00273 {ECO:0000313|EMBL:EPX87700.1};
OS   Rubellimicrobium thermophilum DSM 16684.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Rubellimicrobium.
OX   NCBI_TaxID=1123069 {ECO:0000313|EMBL:EPX87700.1, ECO:0000313|Proteomes:UP000015346};
RN   [1] {ECO:0000313|EMBL:EPX87700.1, ECO:0000313|Proteomes:UP000015346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16684 {ECO:0000313|EMBL:EPX87700.1,
RC   ECO:0000313|Proteomes:UP000015346};
RX   PubMed=24501632; DOI=10.4056/sigs.4247911;
RA   Fiebig A., Riedel T., Gronow S., Petersen J., Klenk H.P., Goker M.;
RT   "Genome sequence of the reddish-pigmented Rubellimicrobium thermophilum
RT   type strain (DSM 16684(T)), a member of the Roseobacter clade.";
RL   Stand. Genomic Sci. 8:480-490(2013).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675}.
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:EPX87700.1}.
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DR   EMBL; AOLV01000004; EPX87700.1; -; Genomic_DNA.
DR   RefSeq; WP_021096385.1; NZ_KE557320.1.
DR   AlphaFoldDB; S9SC60; -.
DR   STRING; 1123069.ruthe_00273; -.
DR   PATRIC; fig|1123069.3.peg.236; -.
DR   HOGENOM; CLU_005070_4_2_5; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000015346; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 4.10.860.10; UVR domain; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001943; UVR_dom.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF145; CLPA/B PROTEASE ATP BINDING SUBUNIT-RELATED; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 2.
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; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
DR   PROSITE; PS50151; UVR; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:EPX87700.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022881};
KW   DNA excision {ECO:0000256|ARBA:ARBA00022769};
KW   DNA repair {ECO:0000256|ARBA:ARBA00022881};
KW   Excision nuclease {ECO:0000256|ARBA:ARBA00022881};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015346};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          115..255
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          528..563
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          918..959
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          524..574
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        938..959
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   959 AA;  105768 MW;  D8BF2942313597DF CRC64;
     MANGTCDICG RPATARVRAS INGRVQNMEL CDQHYREMVR RSGRSASPLE SLFGRHSLFD
     EFFGDGAFGR LFGDSPLRSG SPGLASAGDD DVVDATFGDD TPRRGVRRGA GRSIADRLSE
     QGNKLLQEAA QKAGEFGRSE VDTEHLLLAL TGSEVVRTVL GQFKVDVEDL RRQIEKDAKR
     GDAKGSGEIG VSPRLKDALN RAFIASNELG HSYVGPEHLL IGLAEEGEGL AAAILRKYGL
     TPQALRQQVT KVVGKGAEEG RVEAPSSTPD LDQFSRDLTR LAREGKLDPV IGRAREIETT
     IEVLARRKKN NPVLIGEPGV GKTAIVEGLA QRIVAGEVPE ALRDKRLVEL NINAMVAGSK
     YRGEFEERVQ KILKEITEEK DRLILFIDEI HTIVGAGQGG GEGGLDIANT FKPALARGEL
     NLIGATTLNE YQKYIEKDAA LERRFQPVYV EEPTIAQTIM ILRGLRDTLE AHHKVTITDE
     AIVAAAELSD RYITGRFMPD KAIDLIDQAA ARVKISATAR PVDVQELEAE VAQLRREQDY
     AAARRQFERA AELKKELEQK QKELDELLEV WKRDRASATA EVRADHVAQV VSKITGVPVT
     ELTTEEKDKL LKLEEKLHER VIGQDEAIRA VADAVRLARA GLREGRGPTA TFLFLGPTGV
     GKTELAKTLA EVIFGDQDAM IRIDMSEYGE RHSVARLVGA PPGYVGYEEG GQLTEKVRRR
     PYAVVLLDEI EKAHPDVYNI LLQVFDDGRL TDGKGRVVDF TNTIIIATSN LGADIIQRNL
     RKRGTSEFDE ARQKAELMEV LRGHFRPEFI NRIDEIIVFH SLNQSEIRQI VELQLNRVKR
     TALTQGVELD FDVSVVDHFG AVGFRPEFGA RELRRLIRSE LETELAREML SGRIEDGDKV
     RVAWSPDAQK VVFEKIAKEP GDAKPDDQAA AAEKADAAAS DVVDDDKDEA QSKDDKPTG
//
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