ID Q0I8X1_SYNS3 Unreviewed; 863 AA.
AC Q0I8X1;
DT 03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 126.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=sync_1897 {ECO:0000313|EMBL:ABI45946.1};
OS Synechococcus sp. (strain CC9311).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=64471 {ECO:0000313|EMBL:ABI45946.1, ECO:0000313|Proteomes:UP000001961};
RN [1] {ECO:0000313|EMBL:ABI45946.1, ECO:0000313|Proteomes:UP000001961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9311 {ECO:0000313|EMBL:ABI45946.1,
RC ECO:0000313|Proteomes:UP000001961};
RX PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA Paulsen I.T.;
RT "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT coastal environment.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
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}.
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; CP000435; ABI45946.1; -; Genomic_DNA.
DR RefSeq; WP_011619814.1; NC_008319.1.
DR AlphaFoldDB; Q0I8X1; -.
DR STRING; 64471.sync_1897; -.
DR KEGG; syg:sync_1897; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_3; -.
DR OMA; SKMMQGE; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000001961; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:ABI45946.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ABI45946.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001961};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 5..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 435..527
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 863 AA; 95741 MW; 2C3F7C2091F1FE91 CRC64;
MQPTAEQFTE KAWSAITSAQ QLAQNRRHQQ LESEHLLRAL LDQEGLAGRI LDKAGVSSTA
LQTSVDTFLS QQPALSNAPD SVFLGKGLNA LLDRAETLKQ SYGDSFISIE HLLLALADDG
RCGRQLLSQA GTDTSRLKTA INAVRGSQKV TDQNPEGTYE SLEKYGRDLT SAAREGKLDP
VIGRDEEIRR TIQILSRRTK NNPVLIGEPG VGKTAIVEGL AQRIVNGDVP QALQNRQLIA
LDMGALIAGA KYRGEFEERL KAVLKEVTNS EGQIVLFIDE IHTVVGAGAT GGAMDASNLL
KPMLARGELR CIGATTLDEH RQHIEKDPAL ERRFQQVLVD QPTVEDTISI LRGLKERYEV
HHGVRIADSA LVAAAVLSSR YIADRFLPDK AIDLVDESAA RLKMEITSKP EEIDEIDRKI
LQLEMEKLSL GRESDAASQE RLQRLERELA ELSEQQSTLN AQWQQEKGAI DELSALKEEI
ERVQLQVEQA KRNYDLNKAA ELEYGTLAGL QKQLLAQEQA LVETDDNAEK SLLREEVSED
DIAEVIAKWT GIPVAKLVQS EMEKLLKLED QLHQRVVGQN QAVTAVADAI QRSRAGLSDP
NQPIASFLFL GPTGVGKTEL SKALAAQLFD SEDALVRIDM SEYMEKHTVS RLIGAPPGYV
GYEAGGQLTE AVRRRPYAVI LFDEVEKAHP DVFNVMLQIL DDGRVTDGQG RTVDFTNAVL
ILTSNIGSQS ILDLGGDDSQ HQEMESRVNE ALRNHFRPEF LNRIDDTIIF HSLRRDELRL
IVALQVERLR KRLSERKLDL HISEEATDWL ANAGYDPVYG ARPLKRAIQR ELETPIAKAI
LSGAYEEGSS VQIQVKEERL NLL
//