ID A0A0J7J1Z6_9FLAO Unreviewed; 867 AA.
AC A0A0J7J1Z6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=ACM44_02305 {ECO:0000313|EMBL:KMQ72297.1};
OS Chryseobacterium koreense CCUG 49689.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1304281 {ECO:0000313|EMBL:KMQ72297.1, ECO:0000313|Proteomes:UP000035900};
RN [1] {ECO:0000313|EMBL:KMQ72297.1, ECO:0000313|Proteomes:UP000035900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 49689 {ECO:0000313|EMBL:KMQ72297.1,
RC ECO:0000313|Proteomes:UP000035900};
RX PubMed=15545478; DOI=10.1099/ijs.0.02998-0;
RA Kim M.K., Im W.T., Shin Y.K., Lim J.H., Kim S.H., Lee B.C., Park M.Y.,
RA Lee K.Y., Lee S.T.;
RT "Kaistella koreensis gen. nov., sp. nov., a novel member of the
RT Chryseobacterium-Bergeyella-Riemerella branch.";
RL Int. J. Syst. Evol. Microbiol. 54:2319-2324(2004).
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:KMQ72297.1}.
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DR EMBL; LFNG01000003; KMQ72297.1; -; Genomic_DNA.
DR RefSeq; WP_048498494.1; NZ_LFNG01000003.1.
DR AlphaFoldDB; A0A0J7J1Z6; -.
DR STRING; 1304281.ACM44_02305; -.
DR PATRIC; fig|1304281.5.peg.500; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000035900; 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:KMQ72297.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KMQ72297.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035900};
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 867 AA; 97901 MW; DCFCF36B02F02253 CRC64;
MNLNQFTVKS QEAIQKAQQI AMEFGNQSIE PQHLLEGIFQ ADDSISEFLM KKSEAEVNLI
RERNRESLDK LPKVEGGNIY LSQSANKVLL DAPNIAKKMG DEFVTIEHLW LSLFEVNSEV
SQMLKNMGVT KKGLETAIKE LRKGSKATSA SSEETYQSLN KYAKNFNELA AEGKLDPVIG
RDEEIRRVLQ ILSRRTKNNP ILIGEPGVGK TAIAEGIAHR IISGDIPENL MDKTLYSLDM
GALIAGAKYK GEFEERLKSV INEVIKSDGQ IILFIDEIHT LVGAGGGEGA MDAANILKPA
LARGELRAIG ATTLNEYQKY FEKDKALERR FQKVMVEEPD MESAISILRG IKDKYESHHK
VRIKDEAIIA AVEMSQRYIS DRFLPDKAID LIDEASAKLR MEINSKPEEL DVLDRKLMQM
EIELAAISRE GNDLKVQHLK EDIAKVSEQR NEINAKWLKE KQKSEDLTAI KKDIEALKLE
AERASRAGDY AKVAEIQYGK IKEKEADLEK LELEMQNHQN ELIKEEVTAE NISEVISKWT
GIPVTKLIQS EREKLLHLED ELHKRVVGQD EAITSVADAI RRNRAGLNDE KRPIGSFLFL
GTTGVGKTEL AKALAEFLFD DENNMTRIDM SEYQERHSVS RLVGAPPGYI GYEEGGQLTE
AVRRRPYSVV LLDEIEKAHP DVFNTLLQVL DDGRLTDNKG RVVNFKNSII IMTSNLGSLL
IQENFDEAAR DKDDNVPANV IEKTKEEVFG LLKQTLRPEF VNRIDETVLF QPLNKKEIGK
IVHYQLNSFN KMLEKRGIYM TATEDAIDYI TEKGYDPSFG ARPLKRVLQQ EVLNKLSKEI
LAGKVNDGDR IILDYFDESG LVFRPTE
//