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Database: UniProt
Entry: A0A0C1G322_9FLAO
LinkDB: A0A0C1G322_9FLAO
Original site: A0A0C1G322_9FLAO 
ID   A0A0C1G322_9FLAO        Unreviewed;       868 AA.
AC   A0A0C1G322;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=OA93_09965 {ECO:0000313|EMBL:KIA98433.1};
OS   Flavobacterium sp. KMS.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1566023 {ECO:0000313|EMBL:KIA98433.1, ECO:0000313|Proteomes:UP000031466};
RN   [1] {ECO:0000313|EMBL:KIA98433.1, ECO:0000313|Proteomes:UP000031466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS {ECO:0000313|EMBL:KIA98433.1,
RC   ECO:0000313|Proteomes:UP000031466};
RA   Smith A.K., Newman J.;
RT   "Flavobacterium sp. KMS.";
RL   Submitted (OCT-2014) 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:KIA98433.1}.
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DR   EMBL; JSYP01000008; KIA98433.1; -; Genomic_DNA.
DR   RefSeq; WP_039113036.1; NZ_JSYP01000008.1.
DR   AlphaFoldDB; A0A0C1G322; -.
DR   STRING; 1566023.OA93_09965; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000031466; 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:KIA98433.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KIA98433.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031466};
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..521
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   868 AA;  97438 MW;  D5D9868C3A25D1B4 CRC64;
     MNINKFTIKS QEAIQLSQQL AQKNGQQQIE NEHIFKAIFE VDENVAPFIL KKLNVNVPLF
     LQILDSTIQS FPKVSGGDVM LSRDANKALN EAEIIAQKMN DEYVSIEHLM LAIFDSKSKV
     AQILKDQGVT GKGLKAAIEE LRKGERVTSA SAEETYNSLN KYAKNLNELA RTGKLDPVIG
     RDEEIRRVLQ ILTRRTKNNP MLIGEPGVGK TAIAEGLARR IVNGDVPENL KDKIVFSLDM
     GALIAGAKYK GEFEERLKSV VKEVTAAEGD IVLFIDEIHT LVGAGGGEGA MDAANILKPA
     LARGELRAIG ATTLDEYQKY FEKDKALERR FQKIIIEEPD TESAISILRG IKEKYETHHK
     VQIKDEAIIA AVELSQRYIT NRFLPDKAID LMDEAASKLR MEINSKPEEL DVLDRKIMQL
     EIEIEAIKRE KEESKLKALR MELANLKEER NEIYAKWKSE KDVVDGIQAV KLELENFKHE
     ADRAERDGDY GKVAEIRYGK IKEAQERLDV LLKQMHEYQS GNSLIKEEVT REDIAEVVAK
     WTGIPVMKML QTEREKLLHL EDELHRRVVG QEEAIEAVSD AVRRSRAGLQ DMKKPVGTFL
     FLGTTGVGKT ELAKALAEYL FDDENAMTRI DMSEYQERHS VSRLVGAPPG YVGYDEGGQL
     TEAVRRKPYS VILLDEIEKA HPDTFNILLQ VLDEGRLTDN KGRLADFKNT IIIMTSNMGS
     QIIQEKFENL KGGIEAATEA AKVEVLALLK QTVRPEFINR IDEIVLFPPL TVDNIKQIVG
     LQLKSVTKML ALQGITMDAT PEAVAYLSDK GFDPQFGARP VKRVIQRDVL NQLSKEILAG
     KITTDSIILL DAFDGKLVFR NQTPELAN
//
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