ID J4X290_9FLAO Unreviewed; 861 AA.
AC J4X290;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:EJU30151.1};
GN ORFNames=HMPREF1154_0265 {ECO:0000313|EMBL:EJU30151.1};
OS Capnocytophaga sp. CM59.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=936370 {ECO:0000313|EMBL:EJU30151.1, ECO:0000313|Proteomes:UP000003140};
RN [1] {ECO:0000313|EMBL:EJU30151.1, ECO:0000313|Proteomes:UP000003140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM59 {ECO:0000313|EMBL:EJU30151.1,
RC ECO:0000313|Proteomes:UP000003140};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) 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:EJU30151.1}.
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DR EMBL; ALNN01000030; EJU30151.1; -; Genomic_DNA.
DR RefSeq; WP_009642039.1; NZ_ALNN01000030.1.
DR AlphaFoldDB; J4X290; -.
DR PATRIC; fig|936370.3.peg.1557; -.
DR Proteomes; UP000003140; 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 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..521
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 721..748
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 861 AA; 96701 MW; 569478917AF2E0C1 CRC64;
MNFNNYTIKS QEAIQRAQQL AQGLGQQDIQ VEHIFKGIQE VDNNVLPFIL KKLQVNTTTL
NQAVEKALAS YPKVQGGQMS LSRTAGEVLT EASNIAKKMN DEYVSVEHLL LAIFKIKNQV
GQALKEQGVT EKEFEKVIAE LRKGERVTSA SAEDTYNSLN KYAKNLTQLA HSGKLDPVIG
RDDEIRRVLQ ILSRRTKNNP MLVGEPGVGK TAIAEGLAHR IVNGDVPENL KDKTIYSLDM
GALIAGAKYK GEFEERLKSV VKEVTSSDGN IILFIDEIHT LVGAGGGEGA MDAANILKPA
LARGELRAIG ATTLDEYQKY FEKDKALERR FQKVMVEEPD TESAISILRG IKEKYEAHHK
VRIKDEAIIA AVELSQRYIP NRYLPDKAID LMDEAAAKLR MEINSKPEEL DVLDRKIMQL
EIEIEAIKRE NDDEKLRLLN ADLANLKEER NALFTKWQGE KTLVDEIQAV KNNIEQYKLD
AERAEREGNY GKVAELRYGK IKQEEAKLAD LQKEVDTHEM SMIKEEVTRE DIAEVIAKWT
GVPVTKMMQG EREKLLHLEE ELHKRVVGQE EAIAAVSDAI RRSRAGLQDP KKPIGSFLFL
GTTGVGKTEL AKALAEYLFD DENAMTRIDM SEYQEKHAVS RLVGAPPGYV GYDEGGQLTE
AVRRRPYSVV LLDEIEKAHP DTFNILLQVL DEGRLTDNKG RTADFKNTII IMTSNIGSHL
IQESFEKIKN VEEATEKAKE EVLQLLKQTV RPEFINRIDD IVMFAPLTKA DIKQIVRLQL
GGIIKLVARE NIVLEATPEA IDYLAERGYD PQFGARPVKR VLQKEVMNAL SKEILKGNIK
AGSLILIDSF DNGLVFRNKT E
//
