ID A0A4P9J856_9MICC Unreviewed; 870 AA.
AC A0A4P9J856;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:QCU77320.1};
GN ORFNames=E7744_03135 {ECO:0000313|EMBL:QCU77320.1};
OS Citricoccus sp. SGAir0253.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Citricoccus.
OX NCBI_TaxID=2567881 {ECO:0000313|EMBL:QCU77320.1, ECO:0000313|Proteomes:UP000306924};
RN [1] {ECO:0000313|EMBL:QCU77320.1, ECO:0000313|Proteomes:UP000306924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGAir0253 {ECO:0000313|EMBL:QCU77320.1,
RC ECO:0000313|Proteomes:UP000306924};
RA Schuster S.C.;
RT "The genome of Citricoccus sp. SGAir0253 isolated from tropical air
RT collected in Singapore.";
RL Submitted (APR-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; CP039424; QCU77320.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4P9J856; -.
DR KEGG; cig:E7744_03135; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000306924; 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:UP000306924};
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 COILED 405..499
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 870 AA; 93809 MW; E439CB7978ABFCB2 CRC64;
MDAKFTTKSQ EVLSAAAMNA STLGNPQIEP AHLLKALMDQ RGSVAVAVLK AAGVDPDVVS
TAASTAIKEL PATSGASVAQ AQLSRPGLLV VQAARQQAEA LGDEYVSTEH LLLGLAADAG
KAGAALRDAG GSVEALSAAV KEVRGDSRVT TPDPEGTFQA LEKYGTDLTE MARSGKLDPV
IGRDAEIRRV VQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QRMVAGDVPE SLRGKSLISL
DLGSMIAGAK YRGEFEERLK AVLEEIRQSD GQVVTFIDEI HTVVGAGASE GAMDAGNMLK
PMLARGELRL IGATTLDEYR ENIEKDPALE RRFQQVYVGE PSVDDTIAIL RGLKERYEAH
HKVAIADSAL VAAANLSHRY ISGRQLPDKA IDLVDESASR LRMEIDSAPE EIDQLRRSVD
RLTMEELALA DETDPASVER LASLREEMAN QKEKLAGLTA QWEAEKASLN QAGDLRVRLD
ELRSAAEKAQ RDGDLAEASR ILYGEIPALE KELQAAVEAE NGAPGHGEAT MVSEEVTADD
IAEVISAWTG IPAGRMLQSE QDKLLSMEEH LGERLIGQRA AVASVSDAVR RSRAGISDPD
RPTGSFLFLG PTGVGKTELA KALAEFLFDD DHAMVRLDMS EYSEKHTVAR LVGAPPGYIG
HEEGGQLTEA VRRRPYSVIL LDEVEKAHPE VFDILLQVLD DGRLTDGQGR TVDFRNVILI
LTSNLGSQFL VDPALDDAAK RDAVMKVVHA SFKPEFLNRL DDIIMFDPLS IEDLTRIVDL
QVASLARRLT SRRLELEVTD AAREWLALTG YDPAYGARPL RRLVQREIGD QLARALLGGE
IADGDTVLVD RAPGAADGER DRLVVTRRAG
//