ID A0A0A8X6Z9_9BACI Unreviewed; 866 AA.
AC A0A0A8X6Z9;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMD00020551_3866 {ECO:0000313|EMBL:GAM15708.1};
OS Mesobacillus selenatarsenatis SF-1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=1321606 {ECO:0000313|EMBL:GAM15708.1, ECO:0000313|Proteomes:UP000031014};
RN [1] {ECO:0000313|EMBL:GAM15708.1, ECO:0000313|Proteomes:UP000031014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF-1 {ECO:0000313|EMBL:GAM15708.1,
RC ECO:0000313|Proteomes:UP000031014};
RA Kuroda M., Sei K., Yamashita M., Ike M.;
RT "Whole genome shotgun sequence of Bacillus selenatarsenatis SF-1.";
RL Submitted (JUN-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:GAM15708.1}.
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DR EMBL; BASE01000090; GAM15708.1; -; Genomic_DNA.
DR RefSeq; WP_041967339.1; NZ_BASE01000090.1.
DR AlphaFoldDB; A0A0A8X6Z9; -.
DR STRING; 1321606.SAMD00020551_3866; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000031014; 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 Reference proteome {ECO:0000313|Proteomes:UP000031014};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..150
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 87..114
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 416..530
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 866 AA; 97243 MW; 683B370893578549 CRC64;
MDLNKMTESL QNAFVSAQTL AVQHNHQEVD DTHLLLALLE QDGNLAETLL TGIGLNMDNV
KEALNLTLSK KPQVSGSGVE QGKLYITATL QKVLAQAEKE MKQFEDDYLS VEHVLLAALE
IPGSESGGAM RKLGVSREKL LARIKEVRGN QRVTSQNPEA TYEVLKKYGR DLVEEVRAGK
VDPVIGRDSE IRNVIRILSR KTKNNPVLIG EPGVGKTAIV EGLAQRIVRK DVPEGLKDKT
VFALDMSALI AGAKFRGEFE ERLKAVLNEV KKSEGKILLF IDELHTIVGA GKTEGAMDAG
NMLKPMLARG ELHCIGATTL DEHRKYIEKD PALERRFQQV LVQEPDVEDT VSILRGLKER
FEIHHGVNIH DRALVAAATL SDRYITDRFL PDKAIDLVDE ACAMIRTEID SMPTELDEVT
RRVMQLEIEE AALTKEKDDA SRVRLETLRK ELANLREKAN AMKSRWQKEK EGIQKVQEQR
ELLERLRREL EKAENDYDLN KAAELRHGRI PSLEKELKAL ELEVSKNEGE RLLREEVTEE
EIASIVSRWT GIPVMKLVEG EREKLLKLES ILHERVVGQD EAVSLVSDAV LRARAGIKDP
NRPIGSFIFL GPTGVGKTEL AKTLAQSLFD SEEHIIRIDM SEYMEKHAVS RLIGAPPGYV
GYEEGGQLTE AVRRNPYSVI LLDEVEKAHP EVFNILLQML DDGRVTDSQG RMVDFKNTVI
IMTSNIGSHY LLDRQGGEDE ISSETRDLVM AQLRGHFRPE FLNRVDEIIL FKPLALKEIK
MIVGKLVKTL QGRLADQQIQ LSITDEAKEF LADQGFDPVY GARPLKRFIQ RSVETKLARE
IISGRIKEKS QVEVGVENGD ISLSVK
//
