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
//