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Database: UniProt
Entry: A0A367GRN9_9SPHI
LinkDB: A0A367GRN9_9SPHI
Original site: A0A367GRN9_9SPHI 
ID   A0A367GRN9_9SPHI        Unreviewed;       863 AA.
AC   A0A367GRN9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:RCH56122.1};
GN   ORFNames=DJ568_05085 {ECO:0000313|EMBL:RCH56122.1};
OS   Mucilaginibacter hurinus.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=2201324 {ECO:0000313|EMBL:RCH56122.1, ECO:0000313|Proteomes:UP000253209};
RN   [1] {ECO:0000313|EMBL:RCH56122.1, ECO:0000313|Proteomes:UP000253209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZR32 {ECO:0000313|EMBL:RCH56122.1,
RC   ECO:0000313|Proteomes:UP000253209};
RA   Choi L.;
RT   "Mucilaginibacter hurinus sp. nov., isolated from briquette warehouse
RT   soil.";
RL   Submitted (MAY-2018) 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:RCH56122.1}.
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DR   EMBL; QGDC01000002; RCH56122.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367GRN9; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000253209; 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:UP000253209};
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   863 AA;  96785 MW;  981B4B6140E92F01 CRC64;
     MNFNNFTIKA QEAVQKASEI ATGNQQQAIE NAHLLKGLLL VDENVISYLL KKLNVNLNRL
     TETLDKQIGT FPKVSGSNIY LSSDANAALQ KAQGYLKEFK DEFVSVEHIL LGILASNDKT
     AGVLKDAGVS EKDLKKAIVS LRGDNKVTDQ NAEATYNALN KYARNLNEYA ESGKLDPVIG
     RDEEIRRVIQ ILSRRTKNNP ILVGEPGVGK TAIAEGIAFR IIQGDVPESL KSKVVYSLDM
     GALVAGAKYK GEFEERLKAV IKEVVQSDGD IILFIDEIHT LVGAGGGEGA MDAANILKPA
     LARGELRSIG ATTLNEYQKY VEKDKALERR FQKVMVDEPD AADAISILRG LKERYEAHHK
     VIIRDEAIIA AVEMSQRYIS DRFLPDKAID LMDEAASKLR LEMDSVPEAV DELNRRIMQL
     EIEREAIKRE KDEKKVKELS EEIANLSADR DSLYAKWKGE KDLVDNINQK TEQIENFKLE
     ADQAERAGDY GKVAELRYGR IKEVQDEIEK LKISLQQMQS DSRMLNEEVT ADDIAGVVSR
     WTGIPVSKMI QSEREKLLHL EEELHKRVAG QEEAIEAISD AIRRSRAGLQ DKRKPIGSFI
     FLGTTGVGKT ELAKALAEFL FNDESALVRI DMSEYQERHA VSRLIGAPPG YVGYDEGGQL
     TEAVRRKPYS VVLLDEIEKA HPDVFNILLQ VLDDGRLTDN KGRVVNFKNT IIIMTSNIGS
     NVIQENFQTL DDDNRDEVMA KTKNELFELL RSTIRPEFLN RIDEIIMFTP LSRNEIGAIV
     KLQFKQVQDT LAEMGMTIEA TDEALDWLAQ LGYDPQFGAR PLKRVIQKKI LNELSKQILG
     GKVDKDSTIK LDMFDNQFVF MNS
//
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