ID A0A563VWW7_9CYAN Unreviewed; 872 AA.
AC A0A563VWW7;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:VEP15887.1};
GN ORFNames=H1P_3810002 {ECO:0000313|EMBL:VEP15887.1};
OS Hyella patelloides LEGE 07179.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Hyellaceae;
OC Hyella.
OX NCBI_TaxID=945734 {ECO:0000313|EMBL:VEP15887.1, ECO:0000313|Proteomes:UP000320055};
RN [1] {ECO:0000313|EMBL:VEP15887.1, ECO:0000313|Proteomes:UP000320055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1 {ECO:0000313|EMBL:VEP15887.1};
RA Brito A.;
RL Submitted (JAN-2019) 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; CAACVJ010000314; VEP15887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A563VWW7; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000320055; 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 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:UP000320055};
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 414..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 872 AA; 99004 MW; AE60D426E44F6409 CRC64;
MQPTNPQQFT EKAWQAIVKT ADIAKQNQHQ QIESEHLLKA LIEEEGLATS IFNKADISVA
KVRDKVERFI NSQPKVKNLG ESIYLGRSLD TLLDRADKFR QDFEDEYISI EHIVLGYAKD
DRIGRSLFQE FELNEKQLKE IIKQVRGNQK VTDKNPEGKY QALEKYGREL TELAKAGKLD
PVIGRDEEIR RTIQILSRRT KNNPVLIGEP GVGKTAIVEG LAQRIVNRDV PESLRDRKLV
ALDMGALIAG AKYRGEFEER LKAVLKEVTE SKGNIIMFID EIHTVVGAGA TQGSMDAGNL
LKPMLARGEL RCIGATTLDE YRKYIEKDAA LERRFQSVLV NEPNVVDTIS ILRGLKERYE
VHHGVKISDT ALVAAATLSN RYISDRFLPD KAIDLVDESA AKLKMEITSK PEELDEIDRK
ILQLEMEKLS LQKEEDALSQ ERLQRLDKEL ADFKEEQSEL NAQWQAEKED IDKLNNFKEE
IDRVNLEIQQ AERDYDLNKA AELRYGKLTD LQRQVTEIES TLEEKQSSGR NMLREEVVET
DIAEIISKWT GIPLNKLVES EKAKLLHLED ELHQRVIGQE EAVTAVADSI QRSRAGLADP
LRPTASFIFL GPTGVGKTEL AKALAKNLFD SEEALVRIDM SEYMEKHSVS RLVGAPPGYV
GYEEGGQLTE AIRRRPYSVI LFDEIEKAHA DVFNIMLQIL DDGRLTDSQG RTVDFKNSII
IMTSNIGSQH ILDVAGDDSK YEEMRSRVMG AMRDSFRPEF LNRIDEIIIF HGLTKAQLQP
IVQLQIQGLE KRLAEQKLSL KMSEKAIDFL AELGYDPVYG ARPLKRAIQR YLETSIAKSI
LRGEFQEGDT IFVDVEDERL TFKRLSVEML AN
//