ID A0A1I3R8J1_9FLAO Unreviewed; 862 AA.
AC A0A1I3R8J1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN04487893_10785 {ECO:0000313|EMBL:SFJ42455.1};
OS Myroides guanonis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Myroides.
OX NCBI_TaxID=1150112 {ECO:0000313|EMBL:SFJ42455.1, ECO:0000313|Proteomes:UP000243887};
RN [1] {ECO:0000313|Proteomes:UP000243887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26542 {ECO:0000313|Proteomes:UP000243887};
RA Varghese N., Submissions S.;
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; FORU01000007; SFJ42455.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3R8J1; -.
DR STRING; 1150112.SAMN04487893_10785; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000243887; 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: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 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 Hydrolase {ECO:0000313|EMBL:SFJ42455.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFJ42455.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000243887};
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..521
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 862 AA; 96868 MW; 5604A7DE2E149907 CRC64;
MNTNNFTIKS QEALQQAQVI VQSLGQQQIE NEHIFKGILD VDENVSPFIL KKLNVNVELF
KQMLDATIQS FPKVSGAQIG LSREAATAIS EAQAIAQKNN DEYVSIEYLI LAIFKSKSRV
AQILKDQGVT QKDLEVAIDE LRGGERVTSA SAEETYNSLN KYAKNLNQYV KDGKLDPVIG
RDEEIRRVLQ ILSRRTKNNP MLVGEPGVGK TAIAEGLAHR IVQGDVPENL KDKLVFSLDM
GALIAGAKYK GEFEERLKSV VKEVTNAEGT IILFIDEIHT LVGAGGGEGA MDAANILKPA
LARGELRAIG ATTLDEYQKY FEKDKALERR FQKVMVDEPD TESAISILRG IKEKYETHHK
VRIKDDAIIA AVELSQRYIT NRYLPDKAID LMDEAAAKLR MEINSKPEEL DVLDRKIMQL
EIEIEAIKRE NDEQKLKALG LELANIKEDR NAIFSKWNAE KEVVDKVQSI KQEIEDYKLE
AERAERDGDY GKVAELRYGK IKDSQEELEK LQLQLAEKQE GTSLIKEEVT SEDIAEIVAR
WTGVPVTKML QSEREKLLHL EDELHHRVVG QEEAIEAISD AVRRSRAGLQ DPKKPIGSFL
FLGTTGVGKT ELAKALATYM FDDENAMTRI DMSEYSERHS VSRLVGAPPG YVGYDEGGQL
TEAVRRKPYS VVLLDEIEKA HPDTFNILLQ VLDEGRLTDN KGRLADFKNT IIIMTSNMGS
AIIQEKFDEA DGDIEKASES AKDEVLQVLK QTVRPEFINR IDEIVMFTPL SKKNILDIVD
IQLNGIIKML RTQNIIMDAT EEAKQYLAEK GFDPHYGARP VKRVIQKEVL NKLSKEILSG
NVTAESIILL DCFDNELVFR NK
//