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Database: UniProt
Entry: A0A5C6F6C0_9BACT
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ID   A0A5C6F6C0_9BACT        Unreviewed;       878 AA.
AC   A0A5C6F6C0;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   13-SEP-2023, entry version 13.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:TWU55041.1};
GN   ORFNames=Poly59_13340 {ECO:0000313|EMBL:TWU55041.1};
OS   Rubripirellula reticaptiva.
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rubripirellula.
OX   NCBI_TaxID=2528013 {ECO:0000313|EMBL:TWU55041.1, ECO:0000313|Proteomes:UP000317977};
RN   [1] {ECO:0000313|EMBL:TWU55041.1, ECO:0000313|Proteomes:UP000317977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Poly59 {ECO:0000313|EMBL:TWU55041.1,
RC   ECO:0000313|Proteomes:UP000317977};
RA   Wiegand S., Jogler M., Boedeker C., Pinto D., Vollmers J., Rivas-Marin E.,
RA   Kohn T., Peeters S.H., Heuer A., Rast P., Oberbeckmann S., Bunk B.,
RA   Jeske O., Meyerdierks A., Storesund J.E., Kallscheuer N., Luecker S.,
RA   Lage O.M., Pohl T., Merkel B.J., Hornburger P., Mueller R.-W., Bruemmer F.,
RA   Labrenz M., Spormann A.M., Op Den Camp H., Overmann J., Amann R.,
RA   Jetten M.S.M., Mascher T., Medema M.H., Devos D.P., Kaster A.-K.,
RA   Ovreas L., Rohde M., Galperin M.Y., Jogler C.;
RT   "Deep-cultivation of Planctomycetes and their phenomic and genomic
RT   characterization uncovers novel biology.";
RL   Submitted (FEB-2019) 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:TWU55041.1}.
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DR   EMBL; SJPX01000002; TWU55041.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5C6F6C0; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000317977; 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:UP000317977};
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   COILED          413..531
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   878 AA;  97204 MW;  6AE9308ACB313B67 CRC64;
     MTFRFDKLTT KSQSIVADAQ ARAASLGNPE ILTLHILAAM IDEADGITRP LLDKMKVDIE
     QLTSTVKSEI TRLPAVSGGR QPGIAPELQK AFDASSDAAA SLKDDYVATE HLLLGLTRVD
     CKANRLLKLV GVSDNDVLSA MAEVRGSARV TDQNAESTYQ ALEKFGIDLT QLAAQGKLDP
     VIGRDNEIRR VIQVLSRRTK NNPVLIGQPG VGKTAIAEGL ALRIFEGDVP ASLKDKKVIS
     LDMGALVAGA KFRGDFEERL KSVLREVKDS NGQVVLFIDE LHLVVGAGKA EGSPDAANLL
     KPELARGALR CIGATTLDEY RQNIEKDAAL ERRFQPVYVG EPNAEDTIAI LRGLKSRYES
     HHGVRITDSA IVAAANLSNR YIADRFLPDK AIDLIDEAAS RLAMEKESVP EPIDQIQRRL
     RQLELAHRQL VAEEEDSAVA KRTEIEEEMK TLERELADLR EQWEGEKMGL DDVQAIRQEA
     EALQHKFATL DVEAKQKQQR GESPESIYQE MLDTQAKQNK LEKRLEEIES AEPNDTAEDS
     TDRRRLLRRN VTEDEIAEVV SAWTGVPVSR MLETERAKLL VMEERLHGRV IGQNEAVTAV
     SDAVRRSRSG LQDPNRPIGS FLFLGPTGVG KTELCKALAQ VMFDDESAMV RIDMSEFMER
     HSVSRLIGAP PGYVGYEEGG KLTEAVRRRP YSVLLLDEME KAHPDVFNIL LQVLDDGRLT
     DGHGRTVNFT NTVIVMTSNA GSQVIQQVTE EGGGEDEMRA AVNESLRARF LPEFLNRIDD
     IVIFHPLQKD EIRKIVGLQL ERLADRVKEN GLLIEVSEDA VSEIASVGYD PLYGARPLKR
     VIQREVENPL ATALLKHSYP EGSTVKIDFA DGEFRFSG
//
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