GenomeNet

Database: UniProt
Entry: W6KI27_MAGSQ
LinkDB: W6KI27_MAGSQ
Original site: W6KI27_MAGSQ 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system