ID A0A4U9RNA9_HATHI Unreviewed; 878 AA.
AC A0A4U9RNA9;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:VTQ93509.1};
GN ORFNames=NCTC503_02125 {ECO:0000313|EMBL:VTQ93509.1};
OS Hathewaya histolytica (Clostridium histolyticum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hathewaya.
OX NCBI_TaxID=1498 {ECO:0000313|EMBL:VTQ93509.1, ECO:0000313|Proteomes:UP000308489};
RN [1] {ECO:0000313|EMBL:VTQ93509.1, ECO:0000313|Proteomes:UP000308489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC503 {ECO:0000313|EMBL:VTQ93509.1,
RC ECO:0000313|Proteomes:UP000308489};
RG Pathogen Informatics;
RL Submitted (MAY-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|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; LR590481; VTQ93509.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U9RNA9; -.
DR KEGG; hhw:NCTC503_02125; -.
DR Proteomes; UP000308489; Chromosome 1.
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:UP000308489};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 16..164
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 430..548
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 878 AA; 99978 MW; F354E95A18DAD946 CRC64;
MKSDLNYRKE RAILDIEKLT IKVQKSINEA HGIAVKYNHQ QLESIHLFEA LISEDESLIP
NIFSKMGVSI NKLREKTHME LEKMPKVLGE GAKTSGVYPT RRFEEVFIKA EEISKRFKDS
YISVEHLILA MMELEDKGAV GDILRTFGIT KDGFLKVLLE VRGNQTVDTQ DPEGTYDALS
KYGRNLIQDA KKHKLNPVIG RDDEIRRVIR ILSRRTKNNP VLIGEPGVGK TAIVEGIAER
IVRGDVPDGL KDKIVFSLDM GALIAGAKYR GEFEERLKAV LKEVSSSEGK IILFIDEIHT
IVGAGKTEGS MDAGNLIKPM LARGELHCIG ATTFDEYRKY IEKDKALERR FQQVLVGEPT
VDECITILRG LKEKFEIYHG IRIHDNAIVA AAKLSNRYIN NRFLPDKAID LIDEACAMIR
TEIDSLPEEM DDIRRKIFNL QIEKEALSKE KDEVSKERLK EVERELSNLN ENDIEYTARY
EREKSQIDEV KSLKEKIDNY KADLEKAERE YDLNKVAEIK YGVIPSLEKQ LNEKENQLKG
ENSSLLKQEV TEVEISDIVS NWTGIPVTRL VEGERLKLLR LEEELEERVI GQSEAVKAVS
NAVIRARSGL KDPRRPIGSF IFLGPTGVGK TQLAKTLANN LFDSEDNIIR IDMSEYMEKY
AVSRLIGAPP GYVGYEEGGQ LTEAVIRNPY SVILFDEIEK AHEDVFNIFL QILDDGRLTD
NKGRVVDFKN TIIIMTSNMG SSYLLENMES GEISQEVREE VLDELKFKFK PEFLNRLDDV
IMFKALGVKD IEKIIDIFLE DTKNRLREKS IELKITEKAK SVIAREAYDP IYGARPLKRY
IENNIETVLA REIIKGEIYE GSTAIIDVKN DEIIVNKL
//