ID A0A5S5DSK5_9FLAO Unreviewed; 865 AA.
AC A0A5S5DSK5;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 13-SEP-2023, entry version 13.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=C7447_102189 {ECO:0000313|EMBL:TYP98871.1};
OS Tenacibaculum adriaticum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=413713 {ECO:0000313|EMBL:TYP98871.1, ECO:0000313|Proteomes:UP000323136};
RN [1] {ECO:0000313|EMBL:TYP98871.1, ECO:0000313|Proteomes:UP000323136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18961 {ECO:0000313|EMBL:TYP98871.1,
RC ECO:0000313|Proteomes:UP000323136};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-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. {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:TYP98871.1}.
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DR EMBL; VNIA01000002; TYP98871.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5S5DSK5; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000323136; 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:TYP98871.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TYP98871.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000323136};
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"
SQ SEQUENCE 865 AA; 97277 MW; 6480BD98228B64E0 CRC64;
MNLNNFTIKS QETIQLAQQL AQSYGHNQIE NEHIFKALFQ VDENILPFIL KKLNINIDIV
QQVLDKQLES FAKVSGAELM LSREASKTIN EASIIAKKMN DEYVSIEHLI LAIIKSKSSI
GQALKDQGAS EKLVESAINE LRKGERVTSQ SAEETYNSLN KYAKNLNQLA QDGKLDPVIG
RDEEIRRLLQ ILSRRTKNNP LLVGEPGTGK TAIAEGLAHR IIRGDVPENL KDKVIYSLDM
GALIAGAKYK GEFEERLKAV IKEVTSSDGN IVLFIDEIHT LVGAGGGQGA MDAANILKPA
LARGELRAIG ATTLDEYQKY FEKDKALERR FQKVNVDEPD TESAISILRG IKEKYEAHHK
VRIKDEAIIG AVELSQRYIT NRFLPDKAID LMDEAAAKLR MEINSKPEEL DVLDRKVMQL
EIEIEAIKRE NDEVKLKSLN ADLANLKEER NEINAKWQSE KNIVDSIQNL KTDIESYKLE
AEKAERNGDY GKVAELRYGK IKDAQEELEK QQEVLANQNE NSLIKEEVTY DNIAEVVAKW
TGIPVTKMLQ SEREKLLKLE DELHKRVVGQ EEAIEAVSDA VRRSRSGLQN PNKPIGSFLF
LGTTGVGKTE LAKALAQYLF DDENAMTRID MSEYQERHAV SRLVGAPPGY VGYDEGGQLT
EAVRRKPYSV VLLDEIEKAH PDTFNILLQV LDEGRLTDNK GRIADFKNTI IIMTSNMGSH
IIQEKFENMK GDIDTTMELA KTEVLGLLKQ TVRPEFLNRI DDIIMFTPLS EDNIKQIVQL
QLNGVKKMLI EQNITLDATD EAIDYLAKKG YQPEFGARPV KRVIQKEVMN LLSKEILGGK
ITSNSIVLLD EFDGNLVFRN PSNLT
//