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Database: UniProt
Entry: A0A6B8W4D1_9CORY
LinkDB: A0A6B8W4D1_9CORY
Original site: A0A6B8W4D1_9CORY 
ID   A0A6B8W4D1_9CORY        Unreviewed;       854 AA.
AC   A0A6B8W4D1;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:QGU08404.1};
GN   ORFNames=COCCU_12520 {ECO:0000313|EMBL:QGU08404.1};
OS   Corynebacterium occultum.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=2675219 {ECO:0000313|EMBL:QGU08404.1, ECO:0000313|Proteomes:UP000424462};
RN   [1] {ECO:0000313|EMBL:QGU08404.1, ECO:0000313|Proteomes:UP000424462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2039 {ECO:0000313|EMBL:QGU08404.1,
RC   ECO:0000313|Proteomes:UP000424462};
RA   Schaffert L., Ruwe M., Milse J., Hanuschka K., Ortseifen V., Droste J.,
RA   Brandt D., Schlueter L., Kutter Y., Vinke S., Viehoefer P., Jacob L.,
RA   Luebke N.-C., Schulte-Berndt E., Hain C., Linder M., Schmidt P.,
RA   Wollenschlaeger L., Luttermann T., Thieme E., Hassa J., Haak M.,
RA   Wittchen M., Mentz A., Persicke M., Busche T., Ruckert C.;
RT   "Complete genome sequence of Corynebacterium kalinowskii 1959, a novel
RT   Corynebacterium species isolated from soil of a small paddock in
RT   Vilsendorf, Germany.";
RL   Submitted (NOV-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}.
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DR   EMBL; CP046455; QGU08404.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6B8W4D1; -.
DR   KEGG; cok:COCCU_12520; -.
DR   Proteomes; UP000424462; Chromosome.
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:UP000424462};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          1..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          414..528
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   854 AA;  93506 MW;  4E2F4FB29AB59F48 CRC64;
     MSSFNPTTKT QEALQSALQA ASAKGNPDIR PAHLLVAILE QTDGIAAPVL KATGVDPQVV
     SQEAQRLVDS YPKAEGQNLA NPNFNREALN ALTASQELAG ELGDEYVSTE VLMAGIARGT
     SDAADLLKGR GATYEAIKGT FPSVRGSSKV TSQDPEGQFQ ALEKYSTDLT KLAREGKIDP
     VIGRDAEIRR VVQVLSRRTK NNPVLIGEPG VGKTAIVEGL ARRIVAGDVP ESLKGKTLVS
     LDMGSMVAGA KYRGEFEERL KAVLDEIKAA NGQIVTFIDE LHTIVGAGAS GESAMDAGNM
     IKPLLARGEL HMVGATTLNE YRKYIEKDAA LERRFQQVFV GEPSVEDAIG ILRGLRERYE
     VHHGVRIQDS ALVAAATLSD RYITSRFLPD KAIDLVDEAA SRLRMEIDSS PEEVDELERI
     VRRLEIEEMA LAKETDEAAK LRLEKLRQEL ADEREKLGEL KARWNNEKGA IERFREAKEE
     LEKLRQESEI AEREGDYGKV AELRYGRIPE LEKEVVAAEE SVKEGQNNAM LSEEVTPDTI
     ADVVSNWTGI PAGKMLAGET EKLLDMEGEL GKRVVGQQEA VGAVSDAVRR SRAGIADPNR
     PTGSFLFLGP TGVGKTELAK TLADFLFDDE RAMVRIDMSE YGEKHSVARL VGAPPGYVGY
     DAGGQLTEAV RRRPYTVILF DEVEKAHPDV FDILLQVLDD GRLTDGQGRT VDFRNAVIIL
     TSNLGAGGTR EQMMEAVKRT FKPEFINRLD EVVVFDQLSR EQLGSIVEIQ VAQLAQRLSS
     RRLDLKVSDA ARLWLGERGY DPAYGARPLR RLIQQSIGDQ LAKQLLAGDV RDGDIVHVDV
     ADGGEKLDIR GVRN
//
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