ID A0A0G3GNS7_9CORY Unreviewed; 847 AA.
AC A0A0G3GNS7;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
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:AKK02195.1};
GN ORFNames=CEPID_01550 {ECO:0000313|EMBL:AKK02195.1};
OS Corynebacterium epidermidicanis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1050174 {ECO:0000313|EMBL:AKK02195.1, ECO:0000313|Proteomes:UP000035368};
RN [1] {ECO:0000313|EMBL:AKK02195.1, ECO:0000313|Proteomes:UP000035368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45586 {ECO:0000313|EMBL:AKK02195.1,
RC ECO:0000313|Proteomes:UP000035368};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium epidermidicanis DSM 45586,
RT isolated from the skin of a dog suffering from pruritus.";
RL Submitted (MAY-2015) 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; CP011541; AKK02195.1; -; Genomic_DNA.
DR RefSeq; WP_047239457.1; NZ_CP011541.1.
DR AlphaFoldDB; A0A0G3GNS7; -.
DR STRING; 1050174.CEPID_01550; -.
DR KEGG; cei:CEPID_01550; -.
DR PATRIC; fig|1050174.4.peg.315; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000035368; 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:UP000035368};
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..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 847 AA; 92284 MW; 86B637F32DE90DC3 CRC64;
MNSFNPTTKT QEALQGALQN ASKNGNPDIR PAHLLIAILE QADGIAAPVL QATGADPRVI
IGEAAAIVAK YPSASGANMA NPQFNRDALN ALTAAQELAG ELGDEFVSTE VLLAAIARGE
DDAAKLLHAR GATYDTIKAA FQSVRGSQKV TSQDPEGQFQ ALEKYSTDLT KLAREGKIDP
VIGRDEEIRR VIQVLSRRTK NNPVLIGEPG VGKTAIVEGL ARRIVAGDVP ESLQGKTLIS
LDLGSMVAGA KYRGEFEERL KAVLDEIKAA EGQVITFIDE LHTIVGAGAS GESAMDAGNM
IKPLLARGEL RLVGATTLEE YRKYIEKDAA LERRFQQVYV GEPSVEDAIG ILRGLKERYE
VHHGVRIQDS ALVAAATLSD RYITSRFLPD KAIDLVDEAA SRLRMEIDSS PQEIDALERV
VRRLEVEEMA LEKESDAASK MRLDKLRQEL ADEKERLGEL KARWQNEKGS IDRVRTAKEE
LERLRGESER AERDGDLGRV AELRYGRIPE LEKEVAEAES KVETSMVTEE VTPDTIADVV
SAWTGIPAGK MMQGETEKLL NMEAELGKRV VGQKEAVVAV SDAVRRARAG VADPNRPTGS
FLFLGPTGVG KTELAKALAE FLFDDERAMV RIDMSEYGEK HSVARLVGAP PGYVGYDQGG
QLTEAVRRRP YTVVLFDEVE KAHPDVFDVL LQVLDEGRLT DGQGRTVDFR NTILILTSNL
GAGGTREQMM NAVKASFKPE FVNRLDDVVI FDALSEEQLT SIVDIQVAQL AARLAARRLT
LRVSDSARLW LGERGYDPAY GARPLRRLIQ QAIGDQLAKK LLAGSIVDGD TVHVDVADGG
ETLDLSS
//