ID K9X4Q6_9NOST Unreviewed; 881 AA.
AC K9X4Q6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=Cylst_5650 {ECO:0000313|EMBL:AFZ27650.1};
OS Cylindrospermum stagnale PCC 7417.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC Cylindrospermum.
OX NCBI_TaxID=56107 {ECO:0000313|EMBL:AFZ27650.1, ECO:0000313|Proteomes:UP000010475};
RN [1] {ECO:0000313|EMBL:AFZ27650.1, ECO:0000313|Proteomes:UP000010475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7417 {ECO:0000313|EMBL:AFZ27650.1,
RC ECO:0000313|Proteomes:UP000010475};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Cylindrospermum stagnale PCC 7417.";
RL Submitted (JUN-2012) 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; CP003642; AFZ27650.1; -; Genomic_DNA.
DR RefSeq; WP_015210884.1; NC_019757.1.
DR AlphaFoldDB; K9X4Q6; -.
DR STRING; 56107.Cylst_5650; -.
DR KEGG; csg:Cylst_5650; -.
DR PATRIC; fig|56107.3.peg.6215; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_3; -.
DR OrthoDB; 438311at2; -.
DR Proteomes; UP000010475; 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:UP000010475};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 6..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 433..498
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 881 AA; 99039 MW; C50CB998775ABB16 CRC64;
MQPTDPNKFT DTAWEAIVKS QDIVRAYKQQ QLDVEHLIIA LLEEPSSLAT GILARAEVDP
LRLQQQLEAY TQRQPKVAKS DQLYLGTSLD TLLDRAEANR AKFKDADISE GHILLAFAED
ERIGRRVLKG FNVDIAKLEA AVKTVRTSSP KVMEQSPESR FAALEKFGRD LTEQAKAGKL
DPVIGRDDEI RRVIQVLSRR SKNNPVLIGE PGVGKTAIAE ALAQRMVNGD VPESLKNRQL
ISLDIGSLIA GAKYRGEFED RLKNVLREVI ESNGQIVLFI DELHTVVGTG SNQQGAMDAG
NLLKPMLARG ELRCIGATTL DEYRKYIEKD AALERRFQQV YVDQPSVENT ISILRGLKER
YEVHHNVKIS DLALVAAATL SARYISDRFL PDKAIDLVDE AAAKLKMEIT SKPAELETID
RRLMQLEMEK LSLAGEEKGI AQTRERLERI ELEIATLTIK QQKFNDQWQG EKQLLEAISV
LKKEEDALRV QIEQAERDYD LNKAAQLKYG KLEGVQHDRE IKETQLLEIQ NQGSTLLREQ
VTEADIAEIV AKWTGIPVNR LLESERQKLL QLESHLHQRV IGQEEAVAAV SAAIRRARAG
MKDPGRPIGS FLFMGPTGVG KTELARALAQ FLFDSDDALV RLDMSEYMEK HSVSRLVGAP
PGYIGYEEGG QLSETVRRHP YSVVLLDEVE KAHPDVFNIL LQVLDDGRIT DSQGRTVDFR
NTVIVMTSNI GSEYILDVSG DDTKYDTMRN RVTEALRSHF RPEFLNRVDD IILFHTLNRK
EMRHIIRIQL QRVENLLKEQ KISFDISPAA CDYLVEAGYD PVYGARPLKR AIQREVENAI
ATKLLENTFI SGDTIFIEKG ETGLTFSKKA PVKVTVVQTA T
//