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Database: UniProt
Entry: A0A4Q4B7D2_9FLAO
LinkDB: A0A4Q4B7D2_9FLAO
Original site: A0A4Q4B7D2_9FLAO 
ID   A0A4Q4B7D2_9FLAO        Unreviewed;       869 AA.
AC   A0A4Q4B7D2;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   13-SEP-2023, entry version 14.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:RYH74774.1};
GN   ORFNames=EVU94_07095 {ECO:0000313|EMBL:RYH74774.1};
OS   Flavobacteriaceae bacterium 144Ye.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=2510794 {ECO:0000313|EMBL:RYH74774.1, ECO:0000313|Proteomes:UP000293664};
RN   [1] {ECO:0000313|EMBL:RYH74774.1, ECO:0000313|Proteomes:UP000293664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=144Ye {ECO:0000313|EMBL:RYH74774.1,
RC   ECO:0000313|Proteomes:UP000293664};
RA   Rojas S.M., Lantican N.B., Rosana A.R.R.;
RT   "Draft genome sequence of bacteria isolated from the Benham Bank Seamount
RT   that can produce antibiotic compounds.";
RL   Submitted (JAN-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:RYH74774.1}.
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DR   EMBL; SEHM01000002; RYH74774.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Q4B7D2; -.
DR   Proteomes; UP000293664; 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: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:UP000293664};
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;  97688 MW;  4ECFA653DF104C1A CRC64;
     MNFNNYTIKS QEAIQQAQQL AQSLQHQQIE NEHIFKAITL VDENVLPFIL KKLNVNVQTL
     QQVLDKQLES LPKVSGGDIM LSREAGKSLN EAAIIAKKMN DDYVSVEHLI LAVFKSNSKI
     AQMLKDQGVT EKDLVKAIDE LRQGDRVTSQ SQEDTYNSLN KYAKNLNQLA KDGKLDPVIG
     RDEEIRRILQ ILSRRTKNNP ILVGEPGTGK TAIAEGLAHR IVDGDIPENL VDKQIFALDM
     GALIAGAKYK GEFEERLKAV VKEVTTSEGD IVLFIDEIHT LVGAGKGEGA MDAANILKPA
     LARGELRAIG ATTLDEYQKY FEKDKALERR FQKVMVDEPD TESAISILRG IKEKYETHHK
     VRIKDEAIIG AVELSERYIT NRFLPDKAID LMDEAASKLR MEINSKPEEL DVLDRKIMQL
     EIEIEAIKRE KDEAKLKSLR SDLANLKEER NEIYAKWKSE KEVVDNIQNT KQAIENYKLE
     AERAEREGDY GKVAEIRYGK IKEAQESLDK LQKELQENQS GNSLIKEEVT YDDIAEVVAK
     WTGIPVTKML QSEREKLLKL EDELHKRVVG QEEAIAAVSD AVRRSRAGLQ NPQKPIGTFL
     FLGTTGVGKT ELAKALAEYL FDDENAMTRI DMSEYQERHA VSRLVGAPPG YVGYDEGGQL
     TEAVRRKPYS VVLLDEIEKA HPDTFNILLQ VLDEGHLTDN KGRLADFKNT IIIMTSNMGS
     HVIQERFEAT KDIDAAMEAA KVDVLALLKQ SVRPEFLNRI DDTIMFTPLS KENITAIVGL
     QLKGITKMIA KQGITFDATP EAVEYLAEKG YNPEYGARPV KRVIQKEVLN ELSKEILSGK
     VSTDSIILLD AFDDKLVFRN QGDLVSEEY
//
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