ID W7B4Y1_9LIST Unreviewed; 865 AA.
AC W7B4Y1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=MAQA_03166 {ECO:0000313|EMBL:EUJ20957.1};
OS Listeria aquatica FSL S10-1188.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1265818 {ECO:0000313|EMBL:EUJ20957.1, ECO:0000313|Proteomes:UP000019246};
RN [1] {ECO:0000313|EMBL:EUJ20957.1, ECO:0000313|Proteomes:UP000019246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL S10-1188 {ECO:0000313|EMBL:EUJ20957.1,
RC ECO:0000313|Proteomes:UP000019246};
RX PubMed=24599893; DOI=10.1099/ijs.0.052720-0;
RA den Bakker H.C., Warchocki S., Wright E.M., Allred A.F., Ahlstrom C.,
RA Manuel C.S., Stasiewicz M.J., Burrell A., Roof S., Strawn L., Fortes E.D.,
RA Nightingale K.K., Kephart D., Wiedmann M.;
RT "Listeria floridensis sp. nov., Listeria aquatica sp. nov., Listeria
RT cornellensis sp. nov., Listeria riparia sp. nov. and Listeria grandensis
RT sp. nov., from agricultural and natural environments.";
RL Int. J. Syst. Evol. Microbiol. 64:1882-1889(2014).
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:EUJ20957.1}.
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DR EMBL; AOCG01000003; EUJ20957.1; -; Genomic_DNA.
DR RefSeq; WP_036071108.1; NZ_AOCG01000003.1.
DR AlphaFoldDB; W7B4Y1; -.
DR STRING; 1265818.MAQA_03166; -.
DR PATRIC; fig|1265818.5.peg.638; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000019246; 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 78, MITOCHONDRIAL; 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 Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 414..535
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 865 AA; 97443 MW; DB03F591C335673A CRC64;
MEMQKFTQQV QETIAEAQKL AVEKEHQAID VAHVFKILLQ ESDFAKRVYE VAEVDTEKLN
QKVNEELDKI PAVMGTSVKY GESMSNELYQ LIIRAEEEEK ELQDEFISTE HLLLAVMEQK
ENPVTKEILA EGKTKKTILD AVQAIRGGKR VTSQNAEENY EALSKYGRDL VAEVRSGKLD
PVIGRDTEIR NVIRILSRKT KNNPVLIGEP GVGKTAIVEG LAQRIVRKDV PEGLKDKTII
SLDLGSLIAG AKYRGEFEER LKAVLQEVKE SDGQILLFID EIHTIVGAGK TEGAMDAGNM
LKPMLARGEL HCIGATTLDE YRQYIEKDAA LERRFQKVLV PEPTVEDTVS ILRGLKERFE
IHHGVNIHDN ALVAAATLSN RYITDRFLPD KAIDLIDEAC ATIRVEIDSM PSELDEVTRK
VMQLEIEEAA LKEEKDPASE RRLEMLQREL ADYKEEANKM KSKWENEKGE IGKIREMREQ
IDAMRHELEE AENNYDLTRA AELRHGKIPA AEKELAELEK QNREKTQNED RLLQEAVTEN
EIAEIIGRWT GIPVTKLVEG EREKLLKLSD ALHEKVIGQD QAVDLVSDAV LRARAGIKDP
KRPIGSFIFL GPTGVGKTEL AKALAYNMFD SEDHMIRIDM SEYMEKHSVS RLVGAPPGYV
GYEEGGQLTE AVRRNPYSII LLDEIEKAHP DVFNILLQVL DDGRITDSQG RMVDFKNTVI
IMTSNIGSTM LLERAESGEI SDELEQDVLA TLEASFKPEF LNRVDDIILF KPLTLENIKG
IVEKLVDELQ DRLEAQEIHI AISDEAKSFI AEEAYDPVYG ARPLKRYLVR HVETPLARAI
VSGEVMPHST VEIGLDNGAF TFNTK
//
