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
//