ID D3ER11_ATETH Unreviewed; 867 AA.
AC D3ER11;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=UCYN_12450 {ECO:0000313|EMBL:ADB95911.1};
OS Atelocyanobacterium thalassa (isolate ALOHA).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Atelocyanobacterium;
OC Candidatus Atelocyanobacterium thalassa.
OX NCBI_TaxID=1453429 {ECO:0000313|Proteomes:UP000001405};
RN [1] {ECO:0000313|EMBL:ADB95911.1, ECO:0000313|Proteomes:UP000001405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALOHA {ECO:0000313|Proteomes:UP000001405};
RX PubMed=20173737; DOI=10.1038/nature08786;
RA Tripp H.J., Bench S.R., Turk K.A., Foster R.A., Desany B.A., Niazi F.,
RA Affourtit J.P., Zehr J.P.;
RT "Metabolic streamlining in an open-ocean nitrogen-fixing cyanobacterium.";
RL Nature 464:90-94(2010).
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; CP001842; ADB95911.1; -; Genomic_DNA.
DR RefSeq; WP_012954598.1; NC_013771.1.
DR AlphaFoldDB; D3ER11; -.
DR STRING; 1453429.UCYN_12450; -.
DR KEGG; cyu:UCYN_12450; -.
DR PATRIC; fig|713887.8.peg.1171; -.
DR HOGENOM; CLU_005070_4_0_3; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000001405; 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:UP000001405};
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..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 414..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 867 AA; 99201 MW; 00387C7E1B43329C CRC64;
MQPTDPNKFT LKVWEAIVET PKIAKENKHQ QIETEHLMKF LIKKDELSIR VFNKANVDIN
KVQDITEKFI SNQPKVSNSI ESVYLGYSLD KLFDKSENFR QEFQDNYISI EHILLAYIYD
NRFGIDLFKQ INLSKEHLEK VIKEIRGEKK VIDQNPEVNY EALTKYGRDL TKLAEEGKLD
PVIGRDDEIR RTIQILSRRT KNNPVLIGEP GVGKTAIVEG LAQRIINRDV PESLRDRKLI
VLDMGSLIAG AKYRGEFEER LKAVLKEVID SQGSIILFID EIHTVVGAGA TQGAMDAGNL
LKPMLARGEL RCIGATTLNE YRKYIEKDAA LERRFQSVII DEPNVIDTIS ILRGLKERYE
VHHGVKIADT ALVAAAVLSD RYISDRFLPD KAIDLIDESA AKLKIEITSK PEKLDEIDRK
ILQLEMERLS LNKEEDHLSC ERLKILEKEI SDLKQEQFDL NSRWQTEKTL IDQILKLKKT
IDQVNLEIQQ SERDYDLNKA AELRYGKLST LQKQIKELED KTVNNQNKIL LREEVVPSDI
AEIISRWTGI PLNKLVQSEK EKLLNLEDDL HEKIVGQEEA VTAVADSIQR SRAGLADPKR
PIASFLFLGP TGVGKTELAK ALAKSLFDTE ESIVRIDMSE YMERHTISRL IGAPPGYVGY
DEGGQLSEAI RRHPYAVILF DEIEKAHADI FNIMLQILDD GRLTDSQGRT VNFKNTIIIM
TSNIGSQYIL DVVDDDSRYS EMYSRVVKTV QNNFRPEFLN RIDEMIIFHG LQRSQLRDIV
KLQTQLLSNR LEEQNIYIQL SDSALDFIVN VGYDPVYGAR PLKRAIQKYL ETPIAKLLLK
GEFVGEDTIF VDLKDEILIF TKIAIEN
//
