ID W6KI27_MAGSQ Unreviewed; 861 AA.
AC W6KI27;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:CCQ73196.1};
GN ORFNames=MGMAQ_1273 {ECO:0000313|EMBL:CCQ73196.1};
OS Magnetospira sp. (strain QH-2) (Marine magnetic spirillum (strain QH-2)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Magnetospira.
OX NCBI_TaxID=1288970 {ECO:0000313|EMBL:CCQ73196.1, ECO:0000313|Proteomes:UP000032733};
RN [1] {ECO:0000313|EMBL:CCQ73196.1, ECO:0000313|Proteomes:UP000032733}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QH-2 {ECO:0000313|EMBL:CCQ73196.1,
RC ECO:0000313|Proteomes:UP000032733};
RX PubMed=23841906; DOI=10.1111/1462-2920.12180;
RA Ji B., Zhang S.D., Arnoux P., Rouy Z., Alberto F., Philippe N., Murat D.,
RA Zhang W.J., Rioux J.B., Ginet N., Sabaty M., Mangenot S., Pradel N.,
RA Tian J., Yang J., Zhang L., Zhang W., Pan H., Henrissat B., Coutinho P.M.,
RA Li Y., Xiao T., Medigue C., Barbe V., Pignol D., Talla E., Wu L.F.;
RT "Comparative genomic analysis provides insights into the evolution and
RT niche adaptation of marine Magnetospira sp. QH-2 strain.";
RL Environ. Microbiol. 16:525-544(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. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK.
CC {ECO:0000256|ARBA:ARBA00025613}.
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|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU362034}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; FO538765; CCQ73196.1; -; Genomic_DNA.
DR RefSeq; WP_046020836.1; NZ_FO538765.1.
DR AlphaFoldDB; W6KI27; -.
DR STRING; 1288970.MGMAQ_1273; -.
DR KEGG; magq:MGMAQ_1273; -.
DR HOGENOM; CLU_005070_4_0_5; -.
DR OMA; ERMKAVM; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000032733; Chromosome.
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:UP000032733};
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..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 861 AA; 95165 MW; A0EDE036F6B335FE CRC64;
MEFDKLTERV RGFLQNAQGL AARHHHQQLT PLHILSVLLE DKEGMAAGLI AAAGGDAKAA
RKDCAAELDK LPKVEGAGAG QMYVDSDTAR LFDQARQMAD KAGDEFITAE RLLQAMTLTF
ETPANEVLKQ AKVTPQALNR AVEDMRKGRT ASSATAEDNY DALKKYARDL TAAAEEGRID
PVIGRDEEIR RTIQVLSRRT KNNPVLIGEP GVGKTAVVEG LAQRIVSGDV PEALLTKRLL
VLDLGALVAG AKFRGEFEER LKAVLTEVQS AAGEIILFID EMHTLVGAGA AEGSMDASNL
LKPALARGEL HCVGATTINE YRKHVEKDAA LARRFQPVFV AEPTVEDTVS ILRGIKEKYE
MHHGVRIADA ALVSAASLSN RYISDRFLPD KAIDLVDEAA SRVRMEVDSK PEEVDELDRR
IIQLKIEREA LKKESDSASR SRLERLETEL ADLEQRSGSL TDRWKAEKDH LAEATKLKEK
LDQARIAAER AMREGKLEEA SELQYSLLPE LERRLSEAEG QENTRMVEEA VLESHIASVV
SRWTGIPVDK MLQGEREKLL NMEQALRGRV IGQDEALVAV SDAVRRARAG LQDINRPIGS
FLFLGPTGVG KTELTKALAG FLFDDEQAMV RIDMSEYMEK HAVARLIGAP PGYVGHDEGG
MLTEAVRRRP YQVVLFDEVE KAHPDVFNVL LQVLDDGRLT DGQGRTVDFR NVLIILTSNI
GAEILSEQAD GHDSEEIRPQ VMEMVRQAFR PEFLNRLDEV ILFHRLFREH MGGIVEIQLS
RLSKLLEERK ITIELDDAAK DWLSDAGYDP AYGARPLKRV IQKNLQNALA GLILEDRVKD
GDRVLVSADS NGLTLNGEGG G
//