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Database: UniProt
Entry: E1VYN5_GLUAR
LinkDB: E1VYN5_GLUAR
Original site: E1VYN5_GLUAR 
ID   E1VYN5_GLUAR            Unreviewed;       862 AA.
AC   E1VYN5;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 86.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:CBT76738.1};
GN   OrderedLocusNames=AARI_25210 {ECO:0000313|EMBL:CBT76738.1};
OS   Glutamicibacter arilaitensis (strain DSM 16368 / CIP 108037 / IAM 15318 /
OS   JCM 13566 / NCIMB 14258 / Re117) (Arthrobacter arilaitensis).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Glutamicibacter.
OX   NCBI_TaxID=861360 {ECO:0000313|EMBL:CBT76738.1, ECO:0000313|Proteomes:UP000006878};
RN   [1] {ECO:0000313|EMBL:CBT76738.1, ECO:0000313|Proteomes:UP000006878}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC   {ECO:0000313|Proteomes:UP000006878};
RX   PubMed=21124797; DOI=10.1371/journal.pone.0015489;
RA   Monnet C., Loux V., Gibrat J.F., Spinnler E., Barbe V., Vacherie B.,
RA   Gavory F., Gourbeyre E., Siguier P., Chandler M., Elleuch R., Irlinger F.,
RA   Vallaeys T.;
RT   "The Arthrobacter arilaitensis Re117 genome sequence reveals its genetic
RT   adaptation to the surface of cheese.";
RL   PLoS ONE 5:E15489-E15489(2010).
RN   [2] {ECO:0000313|Proteomes:UP000006878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC   {ECO:0000313|Proteomes:UP000006878};
RA   Genoscope.;
RT   "Complete genome sequence of Arthrobacter arilaitensis (strain DSM 16368 /
RT   CIP 108037 / JCM 13566 / Re117).";
RL   Submitted (JUL-2010) 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; FQ311875; CBT76738.1; -; Genomic_DNA.
DR   RefSeq; WP_013349855.1; NC_014550.1.
DR   AlphaFoldDB; E1VYN5; -.
DR   STRING; 861360.AARI_25210; -.
DR   KEGG; aai:AARI_25210; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_11; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000006878; 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:UP000006878};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          1..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          398..499
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   862 AA;  93707 MW;  D1705064D92B6282 CRC64;
     MDTKLTTKSQ EALSASGMNA STAGNPQIEP AHLLKALLDQ RESVAVALLK TAGMDVDALS
     VKASAVINAL PSTSGSSVAQ AQFSRQLLQV VNNAQETATE MGDTYVSTEH LLIALASDQT
     KAGEALREFG ATRELLVGTL PTIRGDRKVN SPDPEATFQS LEKFGTDMTA LARSGKLDPV
     IGRDREIRRV VQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QRMIAGDVPE SLRGKTLISL
     DLGAMVAGAK YRGEFEERLK SVLEEIKASD GQIVTFIDEI HTVVGAGASE GAMDAGNMLK
     PMLARGELRL IGATTLDEYR ENIEKDPALE RRFAQVYVGE PSVDDTIAIL RGLKERYEAH
     HKVSIADSAL VAASTLSNRY ISGRQLPDKA IDLVDEAASR LRMEIDSAPE EIDELRREVD
     RLTMEELALS DETDPASVER LEALRKDMAD KKEKLDALNS QWEAEKAGLN RVGDLKVKLD
     ELRSQAEKAQ REGDLEKASR LLYGEIPTLQ QELDAAAAAE ADKADVHTMV AEEVTADDIA
     EVISAWTGIP AGRMLQGESQ KLLEMEEVIG QRLMGQKQAV AAVSDAVRRT RAGIADPNRP
     TGSFLFLGPT GVGKTELAKS LADFLFDDPR AMVRIDMSEY SEKHAVSRLV GAPPGYVGYE
     EGGQLTEAVR RRPYSVILLD EVEKAHPEVF DILLQVLDDG RLTDGQGRTV DFRNTILILT
     SNLGSQFLVD QSLEEEAKKS AVMNVVNASF KPEFLNRLDE VILFDPLSIE ELGNIVKLQI
     DLLAQRLADR RLSLIVDPAA SEWLALTGYD PAYGARPLRR LVQREIGDRL AKEILAGTVQ
     DGDAVVVSLD EAGDKLQVAK QG
//
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