GenomeNet

Database: UniProt
Entry: A0A1M4XUJ6_9BACT
LinkDB: A0A1M4XUJ6_9BACT
Original site: A0A1M4XUJ6_9BACT 
ID   A0A1M4XUJ6_9BACT        Unreviewed;       874 AA.
AC   A0A1M4XUJ6;
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=SAMN05444008_10447 {ECO:0000313|EMBL:SHE97179.1};
OS   Cnuella takakiae.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Cnuella.
OX   NCBI_TaxID=1302690 {ECO:0000313|EMBL:SHE97179.1, ECO:0000313|Proteomes:UP000184368};
RN   [1] {ECO:0000313|EMBL:SHE97179.1, ECO:0000313|Proteomes:UP000184368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26897 {ECO:0000313|EMBL:SHE97179.1,
RC   ECO:0000313|Proteomes:UP000184368};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FQUO01000004; SHE97179.1; -; Genomic_DNA.
DR   RefSeq; WP_073041107.1; NZ_MTFE01000010.1.
DR   AlphaFoldDB; A0A1M4XUJ6; -.
DR   STRING; 1302690.BUE76_14415; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000184368; 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:SHE97179.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SHE97179.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184368};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..145
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          397..529
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   874 AA;  98567 MW;  453EB6C9E96856FC CRC64;
     MNLSNFTIKA AEAIQQSQQL AFNGSNSQIE TEHILKALLD QEDSPVEYLL KKNAVNIPQL
     ESRLDQALER LPKVSGEPAQ QISRDGNNVV LRAGAVLKQF KDEFITPEHL LLAIVQGNDN
     TAKLLKDFGV TEKSLVAAIN DLRKGNTVTS QTQETQFNTL KKYAKNLNEM ARQGKLDPVI
     GRDEEIRRTL HILSRRTKNN PILVGEPGVG KTAIAEGLAI RIVNGDVPEN LKSKIIYALD
     MGQLIAGAKY KGEFEERLKG VVKEVATSEG EIILFIDEIH TLVGAGGGEG AMDAANILKP
     ALARGELRAI GATTLNEYQK YFEKDKALER RFQKVMIEEP SMEDAISILR GVKDRYETHH
     HVRIKDEAII AAVELSSRYI TDRFLPDKAI DLIDESAAKL RLEMNSMPEE LDELERRIRQ
     LEIEREAIKR ENDEEKLKEL NTSIANLAVE RDTLKAKWQE EKDLVEKIQN AKAEIESLKL
     QAEQAEREGD YGRVAEIRYG RVKEQEARIN GLQSELNELS QNSRRLMKEE VDAEDIAESI
     AKSTGIPVSK MLQSEREKLL HLETELHHRV VGQEEAITAV ADAIRRSRAG LQDPKKPIGS
     FIFLGTTGVG KTELAKALAE YLFDDEHMMT RIDMSEYQEK HTVSRLVGAP PGYVGYDEGG
     QLTEAVRRKP YQVVLLDEIE KAHPDVWNIM LQVLDDGRLT DNKGRVVNFK NTIIIMTSNM
     GSDIIQENFA DVTERNLDVV LERTKTEVMS RLKETIRPEF LNRVDEIILF QPLMRNEIKG
     IIRIQLNNLK ELVGRNGIQL QFSDYLLDYL SENGFDPQFG ARPLKRLIQK EIVNGLSKKI
     LAGDIDKSHP VLVDVFDGVV VFRNDVEQGV MSEQ
//
DBGET integrated database retrieval system