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Database: UniProt
Entry: A0A4R3VSZ6_9SPHI
LinkDB: A0A4R3VSZ6_9SPHI
Original site: A0A4R3VSZ6_9SPHI 
ID   A0A4R3VSZ6_9SPHI        Unreviewed;       876 AA.
AC   A0A4R3VSZ6;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   13-SEP-2023, entry version 15.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=EDC17_104721 {ECO:0000313|EMBL:TCV08220.1};
OS   Sphingobacterium alimentarium.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=797292 {ECO:0000313|EMBL:TCV08220.1, ECO:0000313|Proteomes:UP000295197};
RN   [1] {ECO:0000313|EMBL:TCV08220.1, ECO:0000313|Proteomes:UP000295197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22362 {ECO:0000313|EMBL:TCV08220.1,
RC   ECO:0000313|Proteomes:UP000295197};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TCV08220.1}.
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DR   EMBL; SMBZ01000047; TCV08220.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4R3VSZ6; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000295197; 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:TCV08220.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TCV08220.1};
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          411..529
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   876 AA;  99341 MW;  CCF76758EE9E46CE CRC64;
     MQLDKFTIKS QEAIQRAQQL AMENEHQAIE CGHMLKGIME VDENVIPFIF KKLSINHQHV
     IAALDGIVTG YAKVSGGQQY LSHTANEALT KAQSAAKSMK DDYVSLEHII IGLMKVDDPV
     ASLLKDSGLN EKDLTSAIKE LRKGGRVTSH SAEDTYNSLS RYAINLNERA QSGKLDPVIG
     RDDEIRRVLQ ILARRSKNNP ILVGEPGVGK TAIAEGIAFR IVNEDVPEDL LSKEIYSLDM
     GALIAGAKYK GEFEERLKTV VKEVTESDGQ IILFIDEIHT LVGAGGGGES AMDAANILKP
     ALARGELRAI GATTLNEFQK YFEKDKALER RFQKVFIDEP TEEDSVSILR GIKERYENYH
     KIRIKDEAIV AAVQLSIRYI SDRYLPDKAI DLIDEAAAHL RLEMKSKPEE IDILDRKIQQ
     LEIEREAFKR EKDKERVKLI SMQLADLQDE RKQLMALWED EKSVVTNIQN IKQAIEDLKY
     KAEKAEREGY LGKVAEIRYG ELPKREELLK QAVAKLQEYE RDGKRLVREE VTAEDIAEVI
     SRWTGIPVSK MLQSEKQKLL HIEEELHRRV VGQDEAIHAV AAAIRRSRTG LSDENRPIGS
     FLFLGTTGVG KTELAKALAE YLFDDEKLMT RIDMSEYQER HAVSRLIGAP PGYVGYDEGG
     QLTEAVRRKP YSVVLLDEIE KAHPDTFNIL LQVLEDGRLT DNKGRIANFK NTIIIMTSNL
     GSDIIRDNFS EITEKNTEDI IDRTRKQLFE LLKTSIRPEF LNRIDEVIMF RPLSKNDLEG
     IIRIQLAHLQ QVLSKQNITF YVTDNCLDYL QKEGFDAQFG ARPLKRLIQR KILDELSVAM
     LEDTVNPDSH IVIDAIDNKI VFREPENENE KLSFEA
//
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