ID W7CJD0_9LIST Unreviewed; 864 AA.
AC W7CJD0;
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=PCORN_00085 {ECO:0000313|EMBL:EUJ33093.1};
OS Listeria cornellensis FSL F6-0969.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1265820 {ECO:0000313|EMBL:EUJ33093.1, ECO:0000313|Proteomes:UP000019254};
RN [1] {ECO:0000313|EMBL:EUJ33093.1, ECO:0000313|Proteomes:UP000019254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL F6-969 {ECO:0000313|Proteomes:UP000019254};
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:EUJ33093.1}.
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DR EMBL; AODE01000001; EUJ33093.1; -; Genomic_DNA.
DR RefSeq; WP_036076475.1; NZ_AODE01000001.1.
DR AlphaFoldDB; W7CJD0; -.
DR STRING; 1265820.PCORN_00085; -.
DR PATRIC; fig|1265820.5.peg.15; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000019254; 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..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 49..112
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 411..572
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 864 AA; 97494 MW; D7A513DD85AE41FA CRC64;
MEMQKFTQQV QETIASAQQL AIEGKQQQID TLHVFAVLLE HSDFTKRVYE VAEVDAKQLL
KTIQNEIEKL PSVTGSNVQY GQAMSSSLYE LVADAEKERQ KLEDDYVSTE HLLLAVMDQK
KSPITEAIGI PKKQLNEAIL QIRGGKRVTT QNAEEQYEAL LKYGRDLVAE VRTGKIDPVI
GRDAEIRNVI RILSRKTKNN PVLIGEPGVG KTAIVEGLAQ RIVRKDVPEG LKDKTIISLD
IGSLIAGAKY RGEFEERLKA VLQEVKDSDG QILLFIDEIH TIVGAGKTDG AMDAGNMLKP
MLARGELHCI GATTLDEYRQ YIEKDPALER RFQKVLVPEP TVEDTVSILR GLKERFEIHH
GVNIHDNALV AAASLSNRYI TDRFLPDKAI DLVDEACATI RVEIDSMPSE LDEVTRKVMQ
LEIEEAALKE EKDPASERRL EMLQKELADY KEEAHKMKSK WESEKHEISQ IREVREQIDH
LRHELEEAEN NYDLNKAAEL RHGRIPEVEK ELARLEEENR EKTANEDRLL QEEVTENEIA
DIVGRWTGIP VAKLVEGERE KLLKLADSLQ EKVIGQENAV QLVSDAVIRA RAGIKDPRRP
IGSFIFLGPT GVGKTELAKA LAFNLFDSED HMIRIDMSEY MEKHAVSRLV GAPPGYIGYE
EGGQLTEAVR RNPYSIILLD EIEKAHPDVF NILLQVLDDG RITDSQGRLI DFKNTVIIMT
SNIGSTMLLE RTVDGEISEK LEEDVLEVLQ ASFKPEFLNR VDDIILFKPL TLDNIKGIVE
KVVAELQVRL AGQEIKITMT DDAKRFIAEE AYDPIYGARP LKRYITRQIE TPLAREIVAG
KIMPHSEVAI TLQDGRFDFE ILGE
//
