ID A0A553H327_9PSED Unreviewed; 854 AA.
AC A0A553H327;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 13-SEP-2023, entry version 15.
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:TRX76146.1};
GN ORFNames=FM069_02855 {ECO:0000313|EMBL:TRX76146.1};
OS Pseudomonas mangiferae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2593654 {ECO:0000313|EMBL:TRX76146.1, ECO:0000313|Proteomes:UP000315235};
RN [1] {ECO:0000313|EMBL:TRX76146.1, ECO:0000313|Proteomes:UP000315235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DMKU_BBB3-04 {ECO:0000313|EMBL:TRX76146.1,
RC ECO:0000313|Proteomes:UP000315235};
RA Srisuk N., Anurat P.;
RT "Pseudomonas mangiferae sp. nov., isolated from bark of mango tree in
RT Thailand.";
RL Submitted (JUL-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:TRX76146.1}.
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DR EMBL; VJOY01000002; TRX76146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A553H327; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000315235; 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:UP000315235};
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 854 AA; 95083 MW; 2FA0A743379CB207 CRC64;
MRIDRLTSKL QLALSDAQSL AVGHDHAAIE PLHLLQALLD QQGGSIRPLL MQVGFDIPAL
RQALTSEIDQ LPKIQNPTGD VNLSQDLARL LNQADRLAQQ KGDQFISSEL VLLAAMDEQT
RLGKLLVAQG VSKKALENAI ANLRGGQAVN DPNAEESRQA LDKYTVDLTK RAEDGKLDPV
IGRDDEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIAEGLA QRIVNGEVPD GLKDKRLLAL
DMGALIAGAK FRGEFEERLK AVLNELSKQE GRIILFIDEL HTMVGAGKAE GAMDAGNMLK
PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVLVDE PSEEDTIAIL RGLKERYEVH
HKVTITDGAI IAAAKLSHRY ITDRQLPDKA IDLIDEAASR IRMEIDSKPE ALDRLDRRLI
QLKVEREALK KEEDEPARKR LAKLEEDIGK LQKEYADLEE IWKSEKAEVQ GSAQLQQQIE
KAKTELEAAR RKGDLNRMAE LQYGVIPDLE RSLQMVDQHG KPENQLLRNK VTDEEIAEVV
SKWTGIPVSK MLEGEREKLL RMEDALHKRV IGQHEAVVAV ANAVRRSRAG LADPNRPSGS
FLFLGPTGVG KTELCKALAE FLFDTEEAMV RIDMSEFMEK HSVARLIGAP PGYVGYEEGG
YLTEAVRRRP YSVVLLDEVE KAHPDVFNVL LQVLDDGRLT DSQGRTVDFR NAVVVMTSNL
GSAQIQELVG DHEAQRAAVM DALSNHFRPE FINRIDEVVV FEPLAREQIA GIADIQLQRL
RKRLAERELN LELSPEALDK LIAVGYDPVY GARPLKRAIQ RWIENPLAQL ILAGQFNPGS
TIAARVEDDE IVFG
//