ID A0A4P7DPB4_9SPHI Unreviewed; 869 AA.
AC A0A4P7DPB4;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:QBR11286.1};
GN ORFNames=E3D81_03485 {ECO:0000313|EMBL:QBR11286.1};
OS Sphingobacterium sp. CZ-2.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=2557994 {ECO:0000313|EMBL:QBR11286.1, ECO:0000313|Proteomes:UP000294533};
RN [1] {ECO:0000313|EMBL:QBR11286.1, ECO:0000313|Proteomes:UP000294533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CZ-2 {ECO:0000313|EMBL:QBR11286.1,
RC ECO:0000313|Proteomes:UP000294533};
RA Cai X.H., Wang R.Y., Hu S.N., Li Y., Chen T., Zhou W.;
RT "Complete genome sequence of Sphingobacterium sp. strain CZ-2T, isolated
RT from tobacco leaf infected with wildfire disease.";
RL Submitted (MAR-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; CP038159; QBR11286.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4P7DPB4; -.
DR KEGG; sphz:E3D81_03485; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000294533; 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:UP000294533};
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 869 AA; 97613 MW; F7A2C98CE55770BC CRC64;
MNFNNFTIKA QEAIQKASEI AVGNQQQAIE PIHILKALLT VDENIIGHLL KKLNVNLNYV
NAEADKQIAA LPKVSGSNVY LSNSANAVLQ KAQSYLKEFN DEFVSIEHIL LALLTANDKA
SALLKDQGVN EKDLKLAIKE LRGNNRVTDQ NAEATYNALG KYARNLNEYA ESGKLDPVIG
RDEEIRRVMQ ILSRRTKNNP ILVGEPGVGK TAIAEGIAHR IIKGDAPENL KSKTVFSLDM
GALIAGAKYK GEFEERLKAV VKEVSDSDGE IILFIDEIHT LVGAGGGEGA MDAANILKPA
LARGELRAIG ATTLNEYQKY FEKDKALERR FQKVMVEEPD TQDAISILRG LKERYETHHK
VRILDEAIIA AVELSQRYIT DRFLPDKAID LVDEAASKLR LEMDSVPESV DELDRRIMQL
EIEREAIKRE NDEKKVKELS ETIANLSNER DSLKAAWQSE KTLVDQVNQE AQNIEDYKLE
AEQAERAGDY GKVAELRYGK IKEAQDAVER LKKELAEKQD SSRMLKEEVT SEDIADVVSK
WTGIPVNKMI QSEREKLLNL EEELHKRVAG QDEAIEAISD AIRRSRAGLS DAKRPIGSFI
FLGTTGVGKT ELAKALAEFL FDDEQALVRI DMSEYQERHA VSRLIGAPPG YVGYDEGGQL
TEAVRRRPYS VVLLDEIEKA HPDVFNILLQ VLDDGHLTDN KGRVVNFKNT IIIMTSNTGS
HIIQENFSKL MDGNREEIIA KTKDEVFELL QKSIRPEFLN RIDEIIMFTP LSRDEIGDIV
RMQFGKVQRQ LAEQNIFLTA TDEALDWLAQ LGYDPVYGAR PLKRVIQKRI LNELSKEILS
GKITSDSVIE LDSFDHQFVF INKDKNKEG
//
