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Database: UniProt
Entry: A0A255RDR6_9BACT
LinkDB: A0A255RDR6_9BACT
Original site: A0A255RDR6_9BACT 
ID   A0A255RDR6_9BACT        Unreviewed;       891 AA.
AC   A0A255RDR6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:OYP38858.1};
GN   ORFNames=CGZ80_01165 {ECO:0000313|EMBL:OYP38858.1};
OS   Rhodopirellula sp. MGV.
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=2023130 {ECO:0000313|EMBL:OYP38858.1, ECO:0000313|Proteomes:UP000236615};
RN   [1] {ECO:0000313|EMBL:OYP38858.1, ECO:0000313|Proteomes:UP000236615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGV {ECO:0000313|EMBL:OYP38858.1,
RC   ECO:0000313|Proteomes:UP000236615};
RA   Araujo J.E., Pylro V.S., Leite L.R., Silva M.C.P., Lemos L.N.,
RA   Lourenco M.V.M., Andreote F.D.;
RT   "Draft Genome Sequence of Rhodopirellula MGV strain isolated from soil of a
RT   Brazilian mangrove.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC       involved in the recovery of the cell from heat-induced damage, in
CC       cooperation with DnaK, DnaJ and GrpE. {ECO:0000256|RuleBase:RU362034}.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00026057}.
CC   -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC       {ECO:0000256|RuleBase:RU362034}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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:OYP38858.1}.
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DR   EMBL; NPDI01000002; OYP38858.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A255RDR6; -.
DR   Proteomes; UP000236615; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 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; IPR017730; Chaperonin_ClpB.
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; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 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; 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|RuleBase:RU362034};
KW   Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236615};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          5..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          529..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          413..464
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   891 AA;  99171 MW;  54B1CD7D75BDB777 CRC64;
     MTFRFDKLTT KAQGLIAEAQ GRAASAGNPD ITSLHLLSAM LDETDGITGA LLEKMNVDSK
     QLTELTRSEL DKTPKVTGGR QPNVSSELQS AFNEAATAAE SLKDEYVATE HLLLGLAKAK
     TKAQSLLSLC GVSADDVLKA ASEVRGSARV TDQNAEETYQ ALQKYGVDLT ELAAQGKLDP
     VIGRDNEIRR VIQVLSRRTK NNPVLIGQPG VGKTAIAEGL ALRIFEADVP TSLKNKRVIA
     LDMGALVAGA KFRGDFEERL KAVLREVKDS NGRVILFIDE LHLVVGAGKA EGSPDAANLL
     KPELARGALR CVGATTLDEY RQHIEKDAAL ERRFQPVYVE EPTVDDTIAI LRGLKPRYES
     HHGVRITDSA LVAAATLANR YITDRFLPDK AIDLVDEATS RLAMEKESVP EPIDRIQRRL
     RQLELAQRQL EDEDQDDVSI VASREDIQSE MDELSRELVD LREQWESEKI GLEGVQSIRQ
     EAETLDHRFA TLDAEAKQTQ LRGENPEAIY REMLEVQSRQ KELRSKLEEI ERRDASADAE
     TEKPEHHRRL LRREVTSDEI AEVVSLWTGV PVNRMLETER AKLLVMEERL HQRVIGQDEA
     VRAVSDAVRR SRSGLADPNR PIGSFLFLGP TGVGKTELCK ALAEIMFDDE HAMVRIDMSE
     FMERHSVARM IGAPPGYVGY EEGGKLTEAV RRRPYTVVLL DEIEKAHPDV FNILLQVLDD
     GRLTDGQGRT VNFANTVIVM TSNAGSQEIQ RIAAENGSED EMHEAVQEAL RARFLPEFLN
     RIDDMVIFKP LDQAEIRQIV RLQLDHLANR LRENGLNLDV TDAALDEVAK VGYDPTYGAR
     PLKRVIQREV QNQLATALLK STFPEGSTIV VDHDGLNFTF STRNEMQPVN V
//
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