ID A0A4Y8URP9_9GAMM Unreviewed; 870 AA.
AC A0A4Y8URP9;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
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:TFH71445.1};
GN ORFNames=E3V39_13140 {ECO:0000313|EMBL:TFH71445.1};
OS Gammaproteobacteria bacterium LSUCC0112.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1778437 {ECO:0000313|EMBL:TFH71445.1, ECO:0000313|Proteomes:UP000297483};
RN [1] {ECO:0000313|EMBL:TFH71445.1, ECO:0000313|Proteomes:UP000297483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LSUCC0112 {ECO:0000313|EMBL:TFH71445.1,
RC ECO:0000313|Proteomes:UP000297483};
RA Coelho J.T., Henson M.W., Thrash J.C.;
RT "Draft genome sequence of strain LSUCC0112, a member of the Order
RT Cellvibrionales from the Gammaproteobacteria Class.";
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:TFH71445.1}.
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DR EMBL; SPIB01000004; TFH71445.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Y8URP9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000297483; 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 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:UP000297483};
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 405..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 870 AA; 96238 MW; 65AD221D56B061C0 CRC64;
MRMEQLTSKL QAALADAQSL ALGNDNNFIE PVHLILALLD QKSGSVRPLL SQTGFNLNAL
KTGLQGILNR LPKVEGTGGD VAMSNELGRL LNQADKLSQK SGDKFISSET VILAAMSDKG
ELGKLLNSFG ITEKALENAI ANLRGGEKVT DADAEDAFQA LSKYCIDLTE RAEKGELDPV
IGRDGEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIINGEVPE GLKGKKILAL
DMGALIAGAK FRGEFEERLK AVLKELSKQE GSVILFIDEI HTMVGAGKAE GSMDAGNMLK
PALARGELHC VGATTLDEYR KYIEKDAALE RRFQKVLVNE PTEEDTIAIL RGLKERYEVH
HGVQITDSAI IAAARLSQRY IPDRQLPDKA IDLIDEAASL IRMEIDSKPE EMDKLERRLI
QLKIECEALK KEEDDASRKR LDKLAEDILR VEKEFSDLDE IWKAEKASVQ GTQSIKSNLE
KARADLETAR RAGDLARMSE LQYGVIPNLE KTLDMSTQAD MMDMQLLRDR VTEEEIADVV
SRWTGIPVSK MLQSDKQKLL QMESALHKRV IGQHEAVAAV ANAVRRSRSG LSDPNRPSGS
FLFLGPTGVG KTELCKALAE FLFDTEEAMV RIDMSEFMEQ HSVARLIGAP PGYVGYEEGG
YLTEAVRRRP YSVLLLDEVE KAHPDVFNIL LQVLDDGRLT DGHGRTVDFR NTVIVMTSNL
GSDRIQDLMS AGVPDEQTYE QVKREVMSVV TRHFRPEFVN RIDETVVFHP LAAAQIRNIA
NIQIASLNKR LQYTDLSIEV SDAVLDKVAA LGYDPIYGAR PLRRAVQNWI ENPLAQKVIG
GDYGPGDRIV VDVSDEGFQF GKREAGSFQP
//
