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Database: UniProt
Entry: A0A0G3GNS7_9CORY
LinkDB: A0A0G3GNS7_9CORY
Original site: A0A0G3GNS7_9CORY 
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
//
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