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Database: UniProt
Entry: A0A1Y5SPW3_9RHOB
LinkDB: A0A1Y5SPW3_9RHOB
Original site: A0A1Y5SPW3_9RHOB 
ID   A0A1Y5SPW3_9RHOB        Unreviewed;       871 AA.
AC   A0A1Y5SPW3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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:SLN43915.1};
GN   ORFNames=PSA7680_02227 {ECO:0000313|EMBL:SLN43915.1};
OS   Pseudoruegeria aquimaris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Pseudoruegeria.
OX   NCBI_TaxID=393663 {ECO:0000313|EMBL:SLN43915.1, ECO:0000313|Proteomes:UP000193409};
RN   [1] {ECO:0000313|EMBL:SLN43915.1, ECO:0000313|Proteomes:UP000193409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7680 {ECO:0000313|EMBL:SLN43915.1,
RC   ECO:0000313|Proteomes:UP000193409};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) 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|ARBA:ARBA00004496,
CC       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; FWFQ01000014; SLN43915.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y5SPW3; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000193409; Unassembled WGS sequence.
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:UP000193409};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          412..492
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   871 AA;  95645 MW;  5F8A2E2B846C3E45 CRC64;
     MNFEKFTERS RGFIQAAQTI AMRESHQRLA PEHILKALMD DDQGLASNLI KRAGGSPERV
     VEALDAALAK MPKVSGDAGQ IYLDSQTAKV LDEAEKIATK AGDSFVTVER ILTALAVVKS
     KAKDALDAGA VTAMKLNTAI NDIRKGRTAD SASAEEGYDA LKKYARDLTE AAREGKIDPI
     IGRDEEIRRT MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIINGDVPE SLRNKKLMSL
     DMGALVAGAK YRGEFEERLK AVLSEVTAAA GEIILFIDEM HQLVGAGKTD GAMDAANLIK
     PALARGELHC VGATTLDEYR KYVEKDAALA RRFQPVMVDE PTVTDTISIL RGIKEKYELH
     HGVRISDSAL VAAATLSHRY ITDRFLPDKA IDLVDEAASR LRMEVDSKPE ELDALDREIL
     QKQIEAEALK KEDDAASKDR LEKLEKELSE LQDKSAALTA KWQAERDKLA KARELKEQLD
     RARAELDIAK REGNLAKAGE LSYGVIPELE RKVAEAESSE DEVLVEEAVR PEQIAQVVER
     WTGIPTSKML EGEREKLLRM EEELGKRVIG QKAAVRAVAN AVRRARAGLN DEARPLGSFL
     FLGPTGVGKT ELTKAVAEFL FDDDSAMVRI DMSEFMEKHA VARLIGAPPG YVGYDEGGVL
     TEAVRRKPYQ VVLFDEVEKA HPDVFNVLLQ VLDDGVLTDG QGRTVDFKQT LIVLTSNLGA
     QALSQLPEGA DSSEAKRDVM DAVRAHFRPE FLNRLDETII FDRLSRDDMD GIVDIQLGLL
     AKRLARRNIT LELDDAARKW LADEGYDPVF GARPLKRVIQ RHLQDPLAEM LLAGDVLDGS
     TVPVTVGADG LIVGDRIAPS NRRPPEATVV H
//
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