ID A0A0R0BY86_9GAMM Unreviewed; 862 AA.
AC A0A0R0BY86;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=ABB26_17035 {ECO:0000313|EMBL:KRG62166.1};
OS Stenotrophomonas humi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=405444 {ECO:0000313|EMBL:KRG62166.1, ECO:0000313|Proteomes:UP000050864};
RN [1] {ECO:0000313|EMBL:KRG62166.1, ECO:0000313|Proteomes:UP000050864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18929 {ECO:0000313|EMBL:KRG62166.1,
RC ECO:0000313|Proteomes:UP000050864};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-2015) 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:KRG62166.1}.
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DR EMBL; LDJI01000039; KRG62166.1; -; Genomic_DNA.
DR RefSeq; WP_057635908.1; NZ_LDJI01000039.1.
DR AlphaFoldDB; A0A0R0BY86; -.
DR STRING; 405444.ABB26_17035; -.
DR PATRIC; fig|405444.3.peg.2669; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000050864; 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 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 862 AA; 95437 MW; 65BC3D7BA7D70D25 CRC64;
MRMDKLTSNF QKALSDAQSL AVGRDNNIIE PVHVLSALLD QTGGSSRPLL AQAGVNVPVL
RERLAESLDA LPKVSGQAGN LSMGNDLSRL LNNTDKLAQQ HNDQFIASEW FLLAAVDDGG
AAGMALRAAG ADKKKIEAAI DKLRGGETVQ SENAEEQRQA LEKYTIDLTA RAESGKLDPV
IGRDEEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIINDEVPE GLRGKRVLSL
DMGALIAGAK FRGEFEERLK AVLSDLSKNE GQIILFIDEL HTMVGAGKGE GAMDAGNMLK
PALARGELHC IGATTLDEYR QYIEKDAALE RRFQKVFVGE PTVEDTIAIL RGLKERYAVH
HGVEITDPAV VAAATLSNRY ITDRQLPDKA IDLMDEAASR IRMEIDSKPE ELDRLERRLI
QLKIQREMLK KEKDEASRKR LADLETDIDT LEREFSDLNE IWKSEKAALQ GATKIKEQVE
RAKLDLEAAQ RRQDFAKMSE IQYGVLPNLE KQLAAAQEVE RKDFRLVQDR VTDEEIAEVV
SRWTGIPVSK MLEGERDKLL RMEDMLHNRV VGQEEAIRVV SDAVRRSRAG LSDPNRPSGS
FLFLGPTGVG KTELTKALAD FLFDSPDAMV RIDMSEFMEK HSVSRLIGAP PGYVGYEEGG
YLTEAVRRRP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVIVMTSNL
GSHQIQDMSG DDSPEAYTQM KAAVMGVVQA HFRPEFINRL DDIVVFHPLD KQQIKQIARI
QMRGLEKRLG ERGLALEVSD SAFDVLSNVG FDPVYGARPL KRAIQAQLEN PLAQKILSGE
FVSGDTIKVE AGGGGHLQFG KG
//
