ID B4WPJ7_SYNS7 Unreviewed; 871 AA.
AC B4WPJ7;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=S7335_1945 {ECO:0000313|EMBL:EDX84248.1};
OS Synechococcus sp. (strain ATCC 29403 / PCC 7335).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=91464 {ECO:0000313|EMBL:EDX84248.1, ECO:0000313|Proteomes:UP000005766};
RN [1] {ECO:0000313|EMBL:EDX84248.1, ECO:0000313|Proteomes:UP000005766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29403 / PCC 7335 {ECO:0000313|Proteomes:UP000005766};
RA Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) 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|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; DS989904; EDX84248.1; -; Genomic_DNA.
DR RefSeq; WP_006453995.1; NZ_DS989904.1.
DR AlphaFoldDB; B4WPJ7; -.
DR STRING; 91464.S7335_1945; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_3; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000005766; 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:UP000005766};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251};
KW Stress response {ECO:0000256|ARBA:ARBA00023016,
KW ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 6..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 413..527
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 871 AA; 97970 MW; CD92AE92992D810D CRC64;
MQINDPNKFT EKVRSALDST IEVVKQSSQQ QLEPEHLMLA LLDQEGLAPR IFQKLGVSVE
DMRSYTQDFI DKQPKVSNSE SVYIGKHTST LLDRADSYRQ KLEDDFISVE HLVFGFVGDE
HFGRGLFKAF GIKENDLTQA ITQIRGTHKV TDQNPEVKYE SLEKYGRDLT EYAREGRLDP
VIGRDDEIRR TIQILSRRTK NNPVLIGEPG VGKTAIAEGL AQRIVRGDVP QSLQDRTLIS
LDMGALIAGA KYRGEFEERL KAVLKEVTES TGQIVLFIDE IHTVVGAGAT QGAMDAGNLL
KPMLARGELR CIGATTLDEY RQHIEKDAAL ERRFQQVYVD QPSVADTVSI LRGLKERYEV
HHGVKIADNA LVAAAALSTR YISDRFLPDK AIDLVDEAAA KLKMEITSKP EELDEVDRKI
LQLEMERLSL QKESDAGSIE RLERLEEELA NLKEEQAELS AQWQSEKDTI GNIQSIKEEI
DHVNVEIEQA ERNYDYNRGA ELKYGKLTKL QDKLSQAEAA LAETQVSGKT LLREEVTEAD
IAEIISKWTG IPLSKLVESE MQKLLNLEDE LHQRVIGQDE AVTAVADSIQ RSRAGLADPD
RPMASFIFLG PTGVGKTELA KALASYLFDT EEAMVRIDMS EYMEKHSVSR LVGAPPGYVG
YDEGGQLTEA VRRRPFAVIL FDEIEKAHPD VFNILLQVLD DGRITDSQGR TVDFTNSIII
MTSNIGSQYI LDIAGDDTQY DEMRSRVTDA LRSQFRPEFL NRIDEIIIFH ALVKSQLRDI
VKIQIKRLEA RLEERKLALK LSDAALDFLA DVGYDPTYGA RPLKRAIQRE IETKIAKAIL
RSEFLPGDTI FVDVENERLS FKRLPAELVT A
//
