ID A0A4Q1CMM8_9BACT Unreviewed; 880 AA.
AC A0A4Q1CMM8;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:RXK62327.1};
GN ORFNames=ESA94_04765 {ECO:0000313|EMBL:RXK62327.1};
OS Lacibacter luteus.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Lacibacter.
OX NCBI_TaxID=2508719 {ECO:0000313|EMBL:RXK62327.1, ECO:0000313|Proteomes:UP000290204};
RN [1] {ECO:0000313|EMBL:RXK62327.1, ECO:0000313|Proteomes:UP000290204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTM-7 {ECO:0000313|EMBL:RXK62327.1,
RC ECO:0000313|Proteomes:UP000290204};
RA Chen W.-M.;
RT "Lacibacter sp. strain TTM-7.";
RL Submitted (JAN-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:RXK62327.1}.
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DR EMBL; SDHW01000001; RXK62327.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q1CMM8; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000290204; 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 78, MITOCHONDRIAL; 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:UP000290204};
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..522
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 880 AA; 98334 MW; 4EC4BB663770BBEB CRC64;
MNLGNFTIKA AEAVQQAQQL AFNVQNTNIE TEHLLKALLD QEESPVEYLL KKNNVTINLV
ETKLDDAINR LPKTSGEAAQ SISREANSVV LRAGAALKSF GDEFVTPEHL LLAIVQGNDS
TAKLLKDAGL TEKGLITAIK DLRKGDTVKS QTQETQFNAL NKYAKNLIEM ARQGKLDPVI
GRDEEIRRTL HILTRRSKNN PILVGEPGVG KTAIAEGLAM RIVNGDVPEN LKSKIIYALD
MGQLIAGAKY KGEFEERLKS VVKEVSTSDG EIILFIDEIH TLVGAGGGEG AMDAANILKP
ALARGELRAI GATTLNEYQK FFEKDKALER RFQKVMIDEP SVEDAVSILR GLKDRYETHH
HVRIKDEAII AAVELSVRYI TDRFLPDKAI DLIDESAAKL RLEMNSMPEE LDKLERQIRQ
LEIEREAIKR ESDEQKLKEL NTEIANLSVE RDTLKAKWKE EKELVEKVQS AKAEIENLKL
QAERAEREGD YGKVAEIRYG KVKEQEAIIA ELSKQLATSS EKRLLKEEVD AEDIAENIAK
MTGIPVSKMM QSEREKLLHL EDELHNRVIG QNEAITAVAD AIRRSRAGLS DPKKPIGSFI
FLGTTGVGKT ELAKALAEYL FDDESMMTRI DMSEYQEKHT VSRLVGAPPG YVGYDEGGQL
TEAVRRKPYS VVLLDEIEKA HPDVWNVLLQ VLDDGRLTDN KGRVVNFKNT IIIMTSNIGS
HLITEAYEGV NTENEIDKAA ERAKLEVMTL LRQTIRPEFL NRVDEIIMFA PLLRKEIKSI
IRIQLNNLKK LVAQSGLQLE FSDYTLEFLA ENGFDPQFGA RPLKRLIQKE IVNGLSRKIL
SGDVDRSQKV IVDVFDGVVV FRNENGHTAS AKGNTKAAVN
//
