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
//