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Database: UniProt
Entry: G0IW36_CYCMS
LinkDB: G0IW36_CYCMS
Original site: G0IW36_CYCMS 
ID   G0IW36_CYCMS            Unreviewed;       871 AA.
AC   G0IW36;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   OrderedLocusNames=Cycma_2517 {ECO:0000313|EMBL:AEL26256.1};
OS   Cyclobacterium marinum (strain ATCC 25205 / DSM 745 / LMG 13164 / NCIMB
OS   1802) (Flectobacillus marinus).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Cyclobacterium.
OX   NCBI_TaxID=880070 {ECO:0000313|EMBL:AEL26256.1, ECO:0000313|Proteomes:UP000001635};
RN   [1] {ECO:0000313|Proteomes:UP000001635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25205 / DSM 745 / LMG 13164 / NCIMB 1802
RC   {ECO:0000313|Proteomes:UP000001635};
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Chertkov O.,
RA   Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Schuetze A.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Cyclobacterium marinum DSM 745.";
RL   Submitted (JUL-2011) 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; CP002955; AEL26256.1; -; Genomic_DNA.
DR   RefSeq; WP_014020549.1; NC_015914.1.
DR   AlphaFoldDB; G0IW36; -.
DR   STRING; 880070.Cycma_2517; -.
DR   KEGG; cmr:Cycma_2517; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_10; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000001635; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000001635};
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          397..529
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   871 AA;  98110 MW;  8BEF8AFC254D6C36 CRC64;
     MDFKQFTIKS QEVIQKALEL CTAEQQQLIE PAHLLKGIVQ VDANVTDFIF QKLGINSGLI
     LQKLDEIINQ YPKVSGQQPY LSNATNEVLT QAKKYLKTFG DEFVAVEHLL LGVLAGSEKV
     AQLLKGQGLN EKKLIEVIKE LRKGNKVTDQ NAESKYRSLE KYSKNLNDLA KKGKIDPVIG
     RDEEIRRVLQ ILARRTKNNP ILLGEPGVGK TAIVEGLAQR IVSGDVPENL KSKTLISLDM
     GLLVAGAKYK GEFEERLKAV IKEVTDSDGE IILFIDEIHT LIGAGGGGEG AMDAANLLKP
     ALARGELHAI GATTLKEYQK YIEKDKALER RFQQVVVDEP DAADAISILR GIKDKYELHH
     GVRIKDDAVI AAVELSQRYI SDRYLPDKAI DLMDEAAAKL RMEIDSLPQE LDELNRRIMQ
     LEIEREAIRR EKNKDKESVL SKELADLSEK RQELKAKWEG EKAVIQGIQR EKENIDKFKI
     EAEQAERSGD FGKVAEIRYG KIVDSEQKLE SFKEQLKVMQ ENSTLLKEEV DSEDIAAVVS
     KWTGIPLSKM IQSEREKLLH LEEELGKRVA GQKEAITALS DAVRRSRAGL QDPKRPIGSF
     IFLGTTGVGK TELAKALAEY LFSDENAMVR IDMSEYQERH AVSRLVGAPP GYVGYDEGGQ
     LTEAVRRKPY SVVLLDEIEK AHPDVFNILL QVLDDGRLTD NKGRIANFKN TIIIMTTNIG
     SHLIQERFES LNESNKEAVL ESTKEEVFNL LKKSVRPEFL NRIDETIMFE PLNRKILRKI
     VDIQWREIQQ RLAESGIEID ATQDVLDYLG EVGFDPQFGA RPLKRTMQRL VLNELSKQIL
     SGYIKNDSAV LVDLDAEKQV YFKNVDHVEI S
//
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