ID A0A1M4XUJ6_9BACT Unreviewed; 874 AA.
AC A0A1M4XUJ6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-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 ORFNames=SAMN05444008_10447 {ECO:0000313|EMBL:SHE97179.1};
OS Cnuella takakiae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Cnuella.
OX NCBI_TaxID=1302690 {ECO:0000313|EMBL:SHE97179.1, ECO:0000313|Proteomes:UP000184368};
RN [1] {ECO:0000313|EMBL:SHE97179.1, ECO:0000313|Proteomes:UP000184368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26897 {ECO:0000313|EMBL:SHE97179.1,
RC ECO:0000313|Proteomes:UP000184368};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FQUO01000004; SHE97179.1; -; Genomic_DNA.
DR RefSeq; WP_073041107.1; NZ_MTFE01000010.1.
DR AlphaFoldDB; A0A1M4XUJ6; -.
DR STRING; 1302690.BUE76_14415; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000184368; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:SHE97179.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SHE97179.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184368};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 397..529
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 874 AA; 98567 MW; 453EB6C9E96856FC CRC64;
MNLSNFTIKA AEAIQQSQQL AFNGSNSQIE TEHILKALLD QEDSPVEYLL KKNAVNIPQL
ESRLDQALER LPKVSGEPAQ QISRDGNNVV LRAGAVLKQF KDEFITPEHL LLAIVQGNDN
TAKLLKDFGV TEKSLVAAIN DLRKGNTVTS QTQETQFNTL KKYAKNLNEM ARQGKLDPVI
GRDEEIRRTL HILSRRTKNN PILVGEPGVG KTAIAEGLAI RIVNGDVPEN LKSKIIYALD
MGQLIAGAKY KGEFEERLKG VVKEVATSEG EIILFIDEIH TLVGAGGGEG AMDAANILKP
ALARGELRAI GATTLNEYQK YFEKDKALER RFQKVMIEEP SMEDAISILR GVKDRYETHH
HVRIKDEAII AAVELSSRYI TDRFLPDKAI DLIDESAAKL RLEMNSMPEE LDELERRIRQ
LEIEREAIKR ENDEEKLKEL NTSIANLAVE RDTLKAKWQE EKDLVEKIQN AKAEIESLKL
QAEQAEREGD YGRVAEIRYG RVKEQEARIN GLQSELNELS QNSRRLMKEE VDAEDIAESI
AKSTGIPVSK MLQSEREKLL HLETELHHRV VGQEEAITAV ADAIRRSRAG LQDPKKPIGS
FIFLGTTGVG KTELAKALAE YLFDDEHMMT RIDMSEYQEK HTVSRLVGAP PGYVGYDEGG
QLTEAVRRKP YQVVLLDEIE KAHPDVWNIM LQVLDDGRLT DNKGRVVNFK NTIIIMTSNM
GSDIIQENFA DVTERNLDVV LERTKTEVMS RLKETIRPEF LNRVDEIILF QPLMRNEIKG
IIRIQLNNLK ELVGRNGIQL QFSDYLLDYL SENGFDPQFG ARPLKRLIQK EIVNGLSKKI
LAGDIDKSHP VLVDVFDGVV VFRNDVEQGV MSEQ
//