ID A0A285ZY73_9SPHI Unreviewed; 865 AA.
AC A0A285ZY73;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN06297358_1634 {ECO:0000313|EMBL:SOD14557.1};
OS Pedobacter xixiisoli.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1476464 {ECO:0000313|EMBL:SOD14557.1, ECO:0000313|Proteomes:UP000219281};
RN [1] {ECO:0000313|EMBL:SOD14557.1, ECO:0000313|Proteomes:UP000219281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12803 {ECO:0000313|EMBL:SOD14557.1,
RC ECO:0000313|Proteomes:UP000219281};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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; OCMT01000002; SOD14557.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285ZY73; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000219281; 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:SOD14557.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SOD14557.1};
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 865 AA; 97456 MW; 6E1EEDF49F7BF92A CRC64;
MNFNNFTIKA QEAVQKASEI AQGNQQQAIE TAHLLKGLLT VDENVISYVL KKLNVNLNAL
SQKLDEDISK FPKVSGSNIY LSSSANSALQ KAQAFLKEFK DEFVSVEHIL LGILAANDIT
SKLLKDQGVN EKDLKKAITE LRGDNRVTDQ NAEATYQALN KYARNLNEYA ESGKLDPVIG
RDEEIRRVIQ ILSRRTKNNP ILIGEPGVGK TAIAEGIAFR IIKGDVPENL KSKVVYSLDM
GSLIAGAKYK GEFEERLKAV VKEVTQSDGE IVLFIDEIHT LVGAGGGEGA MDAANILKPA
LARGELRAIG ATTLDEYQKY LEKDKALERR FQKVMVEEPD TQDSISILRG LKERYETHHK
VRIKDEAIIA AVEMSQRYIA DRFLPDKAID LMDEAASKLR MEMDSVPENV DALDREIMRL
EIEREAIKRE KDENKVKELS EQIANLAAER DEFKAKWQGE KDLVDAINTE IEQIEAYKLE
AEQAERAGDY GKVAELRYGK IKESQDKVEK LKADLESRQS DSRMLKEEVT ADDIAGVVGR
WTGIPVTKLV SSEREKLLNL EEELHKRVAG QDEAIEAISD AIRRSRAGLQ DKRKPIGSFI
FLGTTGVGKT ELAKALAEFL FNDENAMTRI DMSEYQERHA VSRLIGAPPG YVGYDEGGQL
TEAVRRKPYS VVLLDEIEKA HPDVFNILLQ VLDDGRLTDN KGRVVNFKNT IIIMTSNIGS
HLIQDNFKNL DEDNHDEVVA KTKNELFELL KQTIRPEFLN RIDELIMFTP LNRTEIRDIV
SLQFKHVQDT LAEMGITMEA STEALDWLAE LGYDPQFGAR PLKRVIQKRI LNELSKEILA
GKVDKDSKIK LDMFDHQFVF LNEDK
//