ID A0A367GRN9_9SPHI Unreviewed; 863 AA.
AC A0A367GRN9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:RCH56122.1};
GN ORFNames=DJ568_05085 {ECO:0000313|EMBL:RCH56122.1};
OS Mucilaginibacter hurinus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=2201324 {ECO:0000313|EMBL:RCH56122.1, ECO:0000313|Proteomes:UP000253209};
RN [1] {ECO:0000313|EMBL:RCH56122.1, ECO:0000313|Proteomes:UP000253209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZR32 {ECO:0000313|EMBL:RCH56122.1,
RC ECO:0000313|Proteomes:UP000253209};
RA Choi L.;
RT "Mucilaginibacter hurinus sp. nov., isolated from briquette warehouse
RT soil.";
RL Submitted (MAY-2018) 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:RCH56122.1}.
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DR EMBL; QGDC01000002; RCH56122.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367GRN9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000253209; 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:UP000253209};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 410..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 863 AA; 96785 MW; 981B4B6140E92F01 CRC64;
MNFNNFTIKA QEAVQKASEI ATGNQQQAIE NAHLLKGLLL VDENVISYLL KKLNVNLNRL
TETLDKQIGT FPKVSGSNIY LSSDANAALQ KAQGYLKEFK DEFVSVEHIL LGILASNDKT
AGVLKDAGVS EKDLKKAIVS LRGDNKVTDQ NAEATYNALN KYARNLNEYA ESGKLDPVIG
RDEEIRRVIQ ILSRRTKNNP ILVGEPGVGK TAIAEGIAFR IIQGDVPESL KSKVVYSLDM
GALVAGAKYK GEFEERLKAV IKEVVQSDGD IILFIDEIHT LVGAGGGEGA MDAANILKPA
LARGELRSIG ATTLNEYQKY VEKDKALERR FQKVMVDEPD AADAISILRG LKERYEAHHK
VIIRDEAIIA AVEMSQRYIS DRFLPDKAID LMDEAASKLR LEMDSVPEAV DELNRRIMQL
EIEREAIKRE KDEKKVKELS EEIANLSADR DSLYAKWKGE KDLVDNINQK TEQIENFKLE
ADQAERAGDY GKVAELRYGR IKEVQDEIEK LKISLQQMQS DSRMLNEEVT ADDIAGVVSR
WTGIPVSKMI QSEREKLLHL EEELHKRVAG QEEAIEAISD AIRRSRAGLQ DKRKPIGSFI
FLGTTGVGKT ELAKALAEFL FNDESALVRI DMSEYQERHA VSRLIGAPPG YVGYDEGGQL
TEAVRRKPYS VVLLDEIEKA HPDVFNILLQ VLDDGRLTDN KGRVVNFKNT IIIMTSNIGS
NVIQENFQTL DDDNRDEVMA KTKNELFELL RSTIRPEFLN RIDEIIMFTP LSRNEIGAIV
KLQFKQVQDT LAEMGMTIEA TDEALDWLAQ LGYDPQFGAR PLKRVIQKKI LNELSKQILG
GKVDKDSTIK LDMFDNQFVF MNS
//