ID X5H3F1_9RICK Unreviewed; 854 AA.
AC X5H3F1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
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:AHX11076.1};
GN ORFNames=NHE_0106 {ECO:0000313|EMBL:AHX11076.1};
OS Neorickettsia helminthoeca str. Oregon.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Neorickettsia.
OX NCBI_TaxID=1286528 {ECO:0000313|EMBL:AHX11076.1, ECO:0000313|Proteomes:UP000023755};
RN [1] {ECO:0000313|EMBL:AHX11076.1, ECO:0000313|Proteomes:UP000023755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon {ECO:0000313|EMBL:AHX11076.1,
RC ECO:0000313|Proteomes:UP000023755};
RA Lin M., Daugherty S.C., Nagaraj S., Cheng Z., Xiong Q., Lin F.-Y.,
RA Sengamalay N., Ott S., Godinez A., Tallon L.J., Sadzewicz L., Fraser C.M.,
RA Dunning Hotopp J.C., Rikihisa Y.;
RT "Sequencing and Comparison of Genomes and Transcriptome Profiles of Human
RT Ehrlichiosis Agents.";
RL Submitted (MAR-2014) 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. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK.
CC {ECO:0000256|ARBA:ARBA00025613}.
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; CP007481; AHX11076.1; -; Genomic_DNA.
DR RefSeq; WP_038558805.1; NZ_CP007481.1.
DR AlphaFoldDB; X5H3F1; -.
DR STRING; 1286528.NHE_0106; -.
DR KEGG; nhm:NHE_0106; -.
DR HOGENOM; CLU_005070_4_0_5; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000023755; 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 78, MITOCHONDRIAL; 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:UP000023755};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 413..493
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 854 AA; 94585 MW; 7E365B2A7F63B31E CRC64;
MRLDKFTENS AAIIQSAQLD AVSMGHQMLT TLHILKSLIN NTDGLIPQLL EQCNANPEII
LKKISTALQK LPSVHGQGAG HIHLTPDAAQ AIQGAMGIAQ RAQDSFVTVE RLLQGIAAEK
SEASEILKDQ GVSAPKLQQI IDATRGNRKA DSANAESTFN ALKRYTKDLT EVARSGKLDP
VIGRDEEIRR VMQVLSRRTK NNPVLIGDPG VGKTAIVEGL AMRMVAKDVP QNLAGASLLS
LDLGALIAGS KYRGEFEERL KSVINELTDS AGGIILFIDE LHTLVGAGAT DGAMDASNLL
KPALARGEIH CVGATTLDEY KKHIEKDAAL ARRFQPVFVG QPTEEDTISI LRGIKEKYEV
HHGIRIADSA VVSAATLSNR YITDRFLPDK AIDLMDEAAS KIRIESDSKP EVIDELDRKI
IQLKIEAEAL KKEKDANSVS RLEKIRQDLE SLEKKQADLE SVWQSEKSKL KEIQKIKEEL
NEARQSLEVA QRNGDLATAG RLLYGTIRDL EGRLTREEKH AEGTLLKREV TEDDIAAIVA
KWTGIPVEKM MGSEQQKLLN IENALKKQVI GQNEAVEAVS NAVKRARAGI QDANRPLGSF
MFLGSTGVGK TELSKALAKF LFDDESALLR VDMSEYMEKH SVARLIGAPP GYVGYEEGGV
LTEAVRRRPY QVILFDEIEK AHHDVFNILL QVLDEGRLTD SQGHVVDFKN TILILTSNLG
AEVLSETERI TDTEKTQIME IVRKFFRPEF LNRLDEILFF NRLSNEDIGK IAEIQLCKLQ
NLLKSKNLEI EFTQRAKDWI CEQGYHPIYG ARPLKRVIQQ HVQNPLAQII LSGKVAVDGK
ILIDQIDDKL VIQS
//
