ID A0A1I0RDE3_9FLAO Unreviewed; 864 AA.
AC A0A1I0RDE3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN05421841_2495 {ECO:0000313|EMBL:SEW38686.1};
OS Chryseobacterium wanjuense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=356305 {ECO:0000313|EMBL:SEW38686.1, ECO:0000313|Proteomes:UP000199469};
RN [1] {ECO:0000313|EMBL:SEW38686.1, ECO:0000313|Proteomes:UP000199469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17724 {ECO:0000313|EMBL:SEW38686.1,
RC ECO:0000313|Proteomes:UP000199469};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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|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; FOIU01000002; SEW38686.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0RDE3; -.
DR STRING; 356305.SAMN05421841_2495; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199469; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
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 InterPro; IPR001313; Pumilio_RNA-bd_rpt.
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.
DR PROSITE; PS50302; PUM; 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:SEW38686.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SEW38686.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 410..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 864 AA; 97725 MW; BA0419DBC010C6A5 CRC64;
MNLNQYTVKS QEAIQAAQQV AMEFGNQQIE PQHLLEGIFQ VDENISPFLL KKSEADATLV
RERNRENLER LPKVQGGNIY LSQSANKVLL DAPNIAKKMG DEYVTIEHLW LSLLETNSEV
SKMLKDMGVT KSLLEGGIKE LRKGSKATSA SSEETYQSLN KYAKNFNQLA AEGKLDPVIG
RDEEIRRVLQ ILSRRTKNNP ILIGEPGVGK TAIAEGIAHR IISGDIPENL MDKTLYSLDM
GALIAGAKYK GEFEERLKSV VNEVIKSDGQ IILFIDEIHT LVGAGGGEGA MDAANILKPA
LARGELRAIG ATTLNEYQKY FEKDKALERR FQKVMVEEPD TESAISILRG IKDKYEAHHK
VRIKDEAIIA AVEMSQRYIS DRFLPDKAID LIDEASAKLR MEINSKPEEL DVLDRKLMQM
EIELAAISRE GSQTKIDHLK EDISKISEER NEINAKWLKE KQKSEDLTQI KKDIESLKLE
AERASRAGDY AKVAEIQYGK LREKDEELKK LEIEMQNHQN ELIKEEVTSE NISEVIAKWT
GIPVTKLLQS EREKLLNLET ELHHRVVGQD EAIQAVADAI RRNRAGLSDE KKPIGSFLFL
GTTGVGKTEL AKALAEFLFD DENNMTRIDM SEYQERHSVS RLVGAPPGYV GYDEGGQLTE
AVRRRPYSVV LLDEIEKAHP DVFNTLLQVL DDGRLTDNKG RVVNFKNSII IMTSNLGSHI
IQENFENITE ENQDEIVDKT KIEVFDLLKQ TLRPEFLNRI DETVLFQPLR KKEIGKIVQY
QLRGFNDLLA KRNIIMTATQ DALDYLMNKG YDPAFGARPL KRVIQQEVLN KLSREILAGN
VNDGDRITLD YFEETGLVFR PTEK
//
