ID A0A4Y3TRZ3_9PROT Unreviewed; 869 AA.
AC A0A4Y3TRZ3;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:GEB83837.1};
GN ORFNames=AOR01nite_23140 {ECO:0000313|EMBL:GEB83837.1};
OS Acetobacter orleanensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=104099 {ECO:0000313|EMBL:GEB83837.1, ECO:0000313|Proteomes:UP000317617};
RN [1] {ECO:0000313|EMBL:GEB83837.1, ECO:0000313|Proteomes:UP000317617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 13752 {ECO:0000313|EMBL:GEB83837.1,
RC ECO:0000313|Proteomes:UP000317617};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Acetobacter orleanensis NBRC 13752.";
RL Submitted (JUN-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. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK.
CC {ECO:0000256|ARBA:ARBA00025613}.
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|ARBA:ARBA00004496,
CC 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:GEB83837.1}.
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DR EMBL; BJMU01000019; GEB83837.1; -; Genomic_DNA.
DR RefSeq; WP_048836355.1; NZ_NWTP01000016.1.
DR AlphaFoldDB; A0A4Y3TRZ3; -.
DR STRING; 104099.AD949_02355; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000317617; 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 Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 413..493
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 869 AA; 95154 MW; 5E6467A63BE35211 CRC64;
MDIAKFTERS RGFLQAAQTI AIRDFNQQLT PEHLLKAMLD DEEGAASSLI RAAGGNPDAV
RAANEQALAK LPKVQGGGAG QPSATPDLVR VLDAAEQQAQ KAGDSFVAQD RLLVAIAASD
SSAGRALKDN GATPAALDKA ITTIRKGRTV TSENAEANFD ALKKYARDVT EVALAGKLDP
VIGRDEEIRR AIQVLARRSK NNPVLIGEPG VGKTAIVEGL AQRIVNGDVP EALKNKKLLS
LDMGALVAGA KYRGEFEERL KAVLKEIESA EGQVILFIDE MHTLVGAGRT DGAMDASNLI
KPELARGTLH CIGATTLDEY RKYIEKDAAL ARRFQPVFVG EPSVADTISI LRGIKEKYEL
HHGIRITDGA LVSAATLSNR YITDRFLPDK AIDLIDEAAS RLRMQIDSKP EELDELDRRV
IQLKIEREAL RKESDSASKD RLEAVEAELA DLEEKSDAMS AAWHAEKDRV NAVQKLQEQL
DQAKSEVEVA QRKGDLGKAS ELMYGVIPNL QAQIEEETQK SQSDAGKSGL VSEAVTDQDV
ASIVSRWTGV PVDRMLEGER AKLLRMEDDL RKSVVGQEQA LKAVSNAVRR ARAGLQDPNR
PIGSFLFLGP TGVGKTELTK ALARFLFDDE KALLRIDMSE FMEKHAVARL IGAPPGYVGY
EEGGVLTEAV RRRPYQVILF DEVEKAHEDV FNILLQVLDD GRLTDGQGRT VDFRNTIIVL
TSNLGSDVLA HQPDGESTDM VQAQVMKVVR EHFRPEFLNR LDEIILFSRL QKADMTKIVD
IQIRRLQSLL DERKIVLKLD DLAHAWLANE GYDPVYGARP LKRVIQRSLQ NPLAELLLQG
TIHDGEEVKI SANGDGLLIN GQDAAAALA
//