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Database: UniProt
Entry: A0A1M7KVQ9_9BACT
LinkDB: A0A1M7KVQ9_9BACT
Original site: A0A1M7KVQ9_9BACT 
ID   A0A1M7KVQ9_9BACT        Unreviewed;       866 AA.
AC   A0A1M7KVQ9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN05444266_11024 {ECO:0000313|EMBL:SHM69466.1};
OS   Chitinophaga jiangningensis.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=1419482 {ECO:0000313|EMBL:SHM69466.1, ECO:0000313|Proteomes:UP000184420};
RN   [1] {ECO:0000313|EMBL:SHM69466.1, ECO:0000313|Proteomes:UP000184420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27406 {ECO:0000313|EMBL:SHM69466.1,
RC   ECO:0000313|Proteomes:UP000184420};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FRBL01000010; SHM69466.1; -; Genomic_DNA.
DR   RefSeq; WP_073086106.1; NZ_FRBL01000010.1.
DR   AlphaFoldDB; A0A1M7KVQ9; -.
DR   STRING; 1419482.SAMN05444266_11024; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000184420; 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:SHM69466.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SHM69466.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184420};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          398..530
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   866 AA;  97426 MW;  320AF3A79DF19807 CRC64;
     MNLNNFTIKS QEILQKAQQL AFNNQNQAID TGHLLKALLE DQDSPVEYLL KKNDVNTTFL
     NSKLNEQINK YPRIQGGEPG QVLSRDANNV MLRAGASLKE FKDEFVSVEH LLLAILGGSD
     DTAKLLKDAG LTEKGLKAAI KELRKGETVN SQSGGAQYNT LQKYAKNLNE LAREGKLDPV
     IGRDEEIRRT LHILSRRSKN NPILVGEPGV GKTAIVEGLG HRIINGDVPE NLKSKTIYAL
     DMGALMAGAK YRGEFEERLK GVVKEVAESD GEIILFIDEI HTLIGAGAME GAMDAANILK
     PALARGELRA IGATTLNEYQ KYFEKDKALE RRFQKVLVDE PSVEDAISIL RGLKERYESH
     HHVLIKDEAI IAAVELSHRY ITDRFLPDKA IDLIDESAAK LRLEMNSMPE ELDELERRIR
     QLEIEREAIK RENDEDKLSE LAAEISRLSD ERNTFKAKWQ AEKEVVDKIQ NAKAAIENLR
     LEAEQAERNG DFGRVAEIRY GKVKEQEQLV SDLTKDLEDL SANHKRMLKE EVDAEDIAEN
     VAKATGIPVS KMMQSEKDKL LNLEQELHQR VVGQEEAIIA VSDAIRRSRA GLQDPRRPIG
     SFIFLGTTGV GKTELAKALA EYLFDDETMM TRIDMSEYQE KHSVSRLVGA PPGYVGYDEG
     GQLTEAVRRK PYSVVLLDEI EKAHPDTFNI LLQVLDDGRL TDNKGRVVNF KNTIIIMTSN
     MGSNIIQENF ENIDEGNKEE IVDKTKEEVM SLLKATIRPE FLNRVDEVIM FQPLMRDEIK
     GIINIQLQQL KDMVAKNGMI LEFSDYALEY LSVQGYDPQF GARPLKRLIQ KEIINLLSKK
     ILAGDIDKTK PVLIDVFDGV VVVRNK
//
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