ID R6A4Q7_9PROT Unreviewed; 865 AA.
AC R6A4Q7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BN492_00076 {ECO:0000313|EMBL:CDA43789.1};
OS Proteobacteria bacterium CAG:139.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1262986 {ECO:0000313|EMBL:CDA43789.1, ECO:0000313|Proteomes:UP000018405};
RN [1] {ECO:0000313|EMBL:CDA43789.1, ECO:0000313|Proteomes:UP000018405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:139 {ECO:0000313|Proteomes:UP000018405};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDA43789.1}.
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DR EMBL; CBBV010000113; CDA43789.1; -; Genomic_DNA.
DR AlphaFoldDB; R6A4Q7; -.
DR Proteomes; UP000018405; 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:UP000018405};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 412..526
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 865 AA; 97421 MW; 141EC565075EF9DD CRC64;
MRQDQFTTRF QELLGEAQSM AVERSQQYID PLHLLLAVLK DTEGTGRTLL ERSGVRVREL
ERKVKEAIGK LPEVSGAADN VQISRELMAI LNSMEREAER LGDKFISTDL FLLALCDSKC
DAARLAQEEG LNKPSLENAI LSVRGGEKVD NPEAENNREA LKKYTVDLTE KAKEGKLDPV
IGRDDEIRRA MQILQRRSKN NPVLIGEPGV GKTAVVEGLA QRIVNGEVPD TLRNKRVLSL
DMAGLVAGAK YRGEFEERLK ALLKEVVAEE GRIILFIDEI HTVVGAGKTE GAMDAGNMLK
PALSRGELHV IGATTLDEYR KYIEKDPALE RRFQKVIVNE PSVEDTIAIL RGLQEKYEVH
HGVEITDPAI VAAAELSARY ITDRFLPDKA IDLIDEAAAR IKMEIDSKPE ELDKLDRRLI
QLKIEREAVK KEKDEASKKR LSGLEEEIAK LSREYSDLEE IWKKEKNAAL GSKEVRDEID
KLKTKMEELR RSGKYEELAA IQYGKLPELE KQLVKEEKEE TKLYDEKPKL LRTQVGAEEI
AEVVSRATGI PVSKMMEGER QKLLDMAKYI GKRVVGQKEA VDKVVDAILR SRAGLSDPNR
PYGSFLFLGP TGVGKTELTK ALAEFLFDTE DAMIRIDMSE FMEKHSVARL IGAPPGYVGY
EEGGYLTEAV RRKPYSVILL DEVEKAHPDV FNILLQALDD GRMTDGQGRT VDFKNTVIIM
TSNLGSQEIM NRQGEDPEVV KEAVMDEVKK HFRPEFINRI DEIVVFNALD QKAIREIARI
QIRKLAKRME QQNIGLDVTE AALDEIGKVG FDPLFGARPL RRAVQDYLEN QIAVDILKGK
YAPGDTVFVD YVDGKFIFED RKDNR
//