ID M7XJJ7_9BACT Unreviewed; 870 AA.
AC M7XJJ7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=C943_03415 {ECO:0000313|EMBL:EMS34728.1};
OS Mariniradius saccharolyticus AK6.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Mariniradius.
OX NCBI_TaxID=1239962 {ECO:0000313|EMBL:EMS34728.1, ECO:0000313|Proteomes:UP000010953};
RN [1] {ECO:0000313|EMBL:EMS34728.1, ECO:0000313|Proteomes:UP000010953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK6 {ECO:0000313|EMBL:EMS34728.1,
RC ECO:0000313|Proteomes:UP000010953};
RA Vaidya B., Khatri I., Tanuku N.R.S., Subramanian S., Pinnaka A.;
RT "Genome assembly of Mariniradius saccharolyticus AK6.";
RL Submitted (JAN-2013) 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:EMS34728.1}.
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DR EMBL; AMZY02000005; EMS34728.1; -; Genomic_DNA.
DR RefSeq; WP_008624370.1; NZ_AMZY02000005.1.
DR AlphaFoldDB; M7XJJ7; -.
DR STRING; 1239962.C943_03415; -.
DR eggNOG; COG0542; Bacteria.
DR InParanoid; M7XJJ7; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000010953; 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 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:UP000010953};
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..522
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 870 AA; 98033 MW; BDDEE76F76CA08C6 CRC64;
MDFNQFTVKS QEAIQKAAEL AMAQQQQAIE PAHLLKGIFS EDENVIGFIF KKLGVNKAFV
EQKTDEIIRS YPKVTGQQPY LSNAANQVLA KAKDYLKTFG DEFVAIEHLF LAILAGSDRI
SQLLKDQGIS EKPLTEAIKE LRKGNKVTDQ NAESKYRALE KYSKNLNELA KKGKIDPVIG
RDEEIRRVLQ ILARRTKNNP ILLGEPGVGK TAIVEGLAQR IVSGDVPENL KSKTLISLDM
GLLVAGAKYK GEFEERLKAV IKEVTDSDGE IILFIDEIHT LIGAGGGGEG AMDAANLLKP
ALARGELHAI GATTLKEYQK YIEKDKALER RFQAVMVDEP DAADAISILR GIKDKYELHH
GVRIKDDAVI AAVELSQRYI SDRFLPDKAI DLMDEAAAKL RMEIDSLPQE LDELNRRIMQ
LEIEREAIRR ENNKDKEAVL SKEIAELSEK RQSVKAKWES EKAVITGIRT EKEHIDKLKL
EAEQAERAGD FGKVAEIRYG KIVEAEKKLE GYKAQLEEMQ QGSPLLKEEV DNEDIASVVS
KWTGIPLSKM IQSEREKLLH LEDELGRRVA GQREAIAALS DAVRRSRAGL QDPRRPIGSF
IFMGTTGVGK TELAKALAEY LFNDENAMVR IDMSEYQERH AVSRLVGAPP GYVGYDEGGQ
LTEAVRRKPY SVVLLDEIEK AHPDVFNILL QVLDDGRLTD NKGRVANFKN TIIILTTNIG
SHLIQERFAE MEEWNKEEIM EKTKTEVYEL LKKSVRPEFL NRIDETIMFE PLNQKVIRQI
VDIQWKEIQK RLAESNIEIE ATQEVLDYLG RVGFDPTFGA RPLKRTIQRL ILNELSKQIL
AGYIKNDSAV LVELDADNQV YFRNVEAVEV
//