ID K9XFU9_9CHRO Unreviewed; 886 AA.
AC K9XFU9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=Glo7428_2876 {ECO:0000313|EMBL:AFZ31373.1};
OS Gloeocapsa sp. PCC 7428.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Chroococcaceae; Gloeocapsa.
OX NCBI_TaxID=1173026 {ECO:0000313|EMBL:AFZ31373.1, ECO:0000313|Proteomes:UP000010476};
RN [1] {ECO:0000313|EMBL:AFZ31373.1, ECO:0000313|Proteomes:UP000010476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7428 {ECO:0000313|EMBL:AFZ31373.1,
RC ECO:0000313|Proteomes:UP000010476};
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., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Gloeocapsa sp. PCC 7428.";
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; CP003646; AFZ31373.1; -; Genomic_DNA.
DR RefSeq; WP_015189245.1; NC_019745.1.
DR AlphaFoldDB; K9XFU9; -.
DR STRING; 1173026.Glo7428_2876; -.
DR KEGG; glp:Glo7428_2876; -.
DR PATRIC; fig|1173026.3.peg.3076; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_3; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000010476; 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 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:UP000010476};
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..149
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 433..498
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 886 AA; 99370 MW; B069F7945BD830C1 CRC64;
MQPTDPSKFT DKAWEAIVQS QDVTRRFQQQ QMEVEHLMIA LLEDQKGIAH RFLNRSGVEA
SQVLQQLEAF TKRQPKFLGK ADQLYLGRAL DVMLDRAEAA RVTMEDSLIS VEHFLLAFAD
DERIGRRLFR GLNLDKAKLE AAIKAVRGSQ KVTDPTPEAR YEALTKYGRD LTEQAKAGKL
DPVIGRDDEI RRVIQVLSRR SKNNPVLIGE PGVGKTAIAE GLAQRIINGD VPESLKDRQL
IALDIGSLIA GAKYRGEFED RLRSVLREVT DSNGQIVLFI DELHTVVGTG GTTQGAMDAG
NLLKPMLARG ELRCIGATTL DEYRKYIEKD AALERRFQQV FVDQPSVETT ISILRGLKQR
YEVHHSVKIT DSALVAAATL SNRYISDRFL PDKAIDLVDE AAAQLKMEIT SKPSEVEAID
RRLMQLEMEK LSVAGEDQRA AKNRERLERI EQEITALKTK QQELNAQWQG EKQLLDAISA
LKKEENALQV QIEQAERAYD LNKAAQLKYG KLEGVRRDRE AKETMLIDLQ ARGSTLLREE
VTEADIAEIV AKWTGIPVNR LLASERQKLL QLESHLHERV IGQSEAVSAV SAAIRRARAG
MKDPGRPIGS FLFMGPTGVG KTELARALAE FLFDSDDALV RLDMSEYMEK HSVSRLVGAP
PGYVGYEEGG QLSEAIRRRP YSVVLFDEVE KAHPDVFNIL LQVLDDGRIT DSQGRLVDFR
NTVIVMTSNI GSEHILDVSG DDSKYGIMHK RVMDALRSHF RPEFLNRVDD IILFHTLNRS
ELGQIIRIQL KRVQRLLAEQ KLGLELTPAA EAHLVDVGYD PVYGARPLKR AIQRELENPL
ATKLLENAFD EGETILVDYH DGSLTFNSQG KAQSDRSVLT EATRTN
//
