ID A0A1H3WW12_9BACT Unreviewed; 870 AA.
AC A0A1H3WW12;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN05192529_10440 {ECO:0000313|EMBL:SDZ91313.1};
OS Arachidicoccus rhizosphaerae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Arachidicoccus.
OX NCBI_TaxID=551991 {ECO:0000313|EMBL:SDZ91313.1, ECO:0000313|Proteomes:UP000199041};
RN [1] {ECO:0000313|EMBL:SDZ91313.1, ECO:0000313|Proteomes:UP000199041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vu-144 {ECO:0000313|EMBL:SDZ91313.1,
RC ECO:0000313|Proteomes:UP000199041};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNQY01000004; SDZ91313.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3WW12; -.
DR STRING; 551991.SAMN05192529_10440; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199041; 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 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 Hydrolase {ECO:0000313|EMBL:SDZ91313.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SDZ91313.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199041};
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 399..524
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 870 AA; 97672 MW; C05A56973374B5CD CRC64;
MNPNNYTIKA QELIQAAQQI AYNNGDLNIE TNHLLLALLG EKESAIEFLL KKNDVNIAYT
EQKIRDSLSR LPKAASGEPA QQVGREMNNT LLRAAKDISQ FGDEFINPEH LLLALVQGSD
DTAKILKDAG LTQKGLVAAI KDLRQGAGSV NSQTANQEVG SLKKYAKNLN ELAQAGKLDP
VIGRDEEIRR TLHILSRRSK NNPILVGEPG VGKTAIVEGL AHRIINGDVP ENLKSKIIYS
LDMGLLIAGA KYKGEFEERL KGVIKDVATS DGEIILFIDE IHTLVGAGGG EGAMDAANIL
KPALARGDLR AIGATTLNEY QKFFEKDKAL ERRFQKVMVD EPTIEDAVSI LRGLKERYET
HHHVLIRDEA IIAAVELSNR YITDRFLPDK AIDLIDESAA KLRLEMNSMP EELDELERKI
RQLEIEREAI KRENDQAKLK ELNTNIGNLM VERDTYKAKW QQEKEVVEKM QNAKAAIDSL
KLEAEKAERE GDYGKVAEIR YGKIKEQQEI IDQTNHELQD ISEKRLLKEE VDAEDIAENV
AKATGIPVSR MLQSEKDKLL HLEDHLHQRV VGQQEAITAV SDAIRRSRAG LGDPKRPIGS
FIFLGTTGVG KTELAKALAE FLFDDESMMT RIDMSEYQEK HSVSRLVGAP PGYVGYEEGG
QLTEAVRRKP YSVVLFDEIE KAHPDVFNIL LQVLDDGHLT DNKGRTVNFK NTIIIMTSNI
GSHLIMDAFE NHQDDIDKAE QVAKDEVMNL LKETIRPEFL NRIDEIVMFH PLLKKEIKNI
INIQLRQLKR QIAQGGIHID FSDYVMDYLS ENGYDIQFGA RPLKRFIQKA IVNPLSKKIL
AGEIDRDHPV LVDVFDGIVV FRNEEQVASK
//