ID A0A4R3IAH7_9GAMM Unreviewed; 867 AA.
AC A0A4R3IAH7;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BCF53_103178 {ECO:0000313|EMBL:TCS42517.1};
OS Reinekea marinisedimentorum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Saccharospirillaceae; Reinekea.
OX NCBI_TaxID=230495 {ECO:0000313|EMBL:TCS42517.1, ECO:0000313|Proteomes:UP000295793};
RN [1] {ECO:0000313|EMBL:TCS42517.1, ECO:0000313|Proteomes:UP000295793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15388 {ECO:0000313|EMBL:TCS42517.1,
RC ECO:0000313|Proteomes:UP000295793};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TCS42517.1}.
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DR EMBL; SLZR01000003; TCS42517.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R3IAH7; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000295793; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:TCS42517.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TCS42517.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000295793};
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..461
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 867 AA; 96536 MW; 9C950E260ECEDE52 CRC64;
MRIDKLTSKF QLALADAQSL ALGHDNQYIE PVHVMSALLN QDGGSIRPLL AKVGANTNQL
RSELSEAIER LPSVTGDAGD VHISNDLNRL FNQVEKLAQK RNDQYISSEL FLLAAIEEKG
TLGELLKSAG ATKAAVEKAI DEVRGGQTVN DPNAEEQRQA LEKYTIDLTE RAEQGKLDPV
IGRDDEIRRV IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE GLKNRRLLSL
DMAALIAGAK FRGEFEERLK AVLNDVSKQE GAIILFIDEI HTMVGAGKAD GAMDAGNMLK
PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVLVDE PTQEDTIAIL RGLKEKYELH
HGVDITDSAI VSAVTLSTRY ITDRQLPDKA IDLIDEAGSR IRMEIDSMPE EMDKLDRRLI
QLKMEREALK KEKDQASQKR LELLEDDIGG LEKEFSDLEE IWKAEKASLQ GATHVKEELD
RARIDLEAAH RAGDLARMSE LQYGRIPELE KQLAGAQAAE SNEMTLLRNN VTEEEIAEVV
SRWTGIPVSK MLEGEREKLL HMEEALGKRV IGQEEAIEAV SDAIRSSRAG LSDPKRPNGC
FLFLGPTGVG KTELTKALAE FLFDTEDSMV RIDMSEFMEK HSVARLIGAP PGYVGYEEGG
YLTEAVRRRP YAVILLDEVE KAHPDVFNIL LQVMDDGRLT DGQGRTVDFR NTVIVMTSNL
GSQLIQELAG DEHYEQMKES VMEVVGQHFR PEFINRLDET VVFHPLRQNE IRDISRIQLA
YLQTRMAENE LALEVDDSVI DLIAEAGFDP LFGARPLKRV IKARIEKELA KQILGGKFKP
GDTVVASRDD KNIVFSVVAN AEVVEED
//
