ID A0A4U0P7S2_9SPHI Unreviewed; 865 AA.
AC A0A4U0P7S2;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:TJZ63410.1};
GN ORFNames=FAZ15_03770 {ECO:0000313|EMBL:TJZ63410.1};
OS Sphingobacterium olei.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=2571155 {ECO:0000313|EMBL:TJZ63410.1, ECO:0000313|Proteomes:UP000306808};
RN [1] {ECO:0000313|EMBL:TJZ63410.1, ECO:0000313|Proteomes:UP000306808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAL-9 {ECO:0000313|EMBL:TJZ63410.1,
RC ECO:0000313|Proteomes:UP000306808};
RA Liu B.;
RT "Sphingobacterium olei sp. nov., isolated from oil-contaminated soil.";
RL Submitted (APR-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:TJZ63410.1}.
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DR EMBL; SUME01000001; TJZ63410.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U0P7S2; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000306808; 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:UP000306808};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 403..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 865 AA; 97312 MW; 093516F13E0B2350 CRC64;
MNFNNYTIKA QEAVQKASEI AKGNQQQSVE PAHLLKALLT VDEHVVSHLL KKLNVNISYV
TAEVTKQIEA LPKVSGTNIY ISNNSVAVLQ KAQSYLKEFN DEFVSIEHIL LGLLSANDKV
SSLLKDQGVN EKDLKLAIKE LRGSSRVTDQ NAEATYNALG KYARNLNEYA ESGKLDPVIG
RDDEIRRVIQ ILSRRTKNNP ILVGEPGVGK TAIAEGIAHR IIKGDAPENL KTKTVYSLDM
GALIAGAKYK GEFEERLKAV VKEVTESDGE IILFIDEIHT LVGAGGGEGA MDAANILKPA
LARGELRAIG ATTLNEYQKY FEKDKALERR FQKVMVEEPD TQDAVSILRG LKERYEMHHK
VRILDESIIA AVELSQRYIT DRFLPDKAID LIDEAASKLR LEMDSVPEAV DELERRIMQL
EIEREAIKRE NDNKKVAELS EIIANLSNER DSLKAAWQSE KHLVDRVNQE IQNIEDYKLE
AEQAERAGDY GKVAELRYGK IKDAQDATEK LKAELAEKQQ GSRMLKEEVT SEDIADVVSR
WTGIPMNKMV QSERQKLLTL EEELHKRVAG QDEAIEAISD AIRRSRAGLS DAKRPIGSFI
FLGTTGVGKT ELAKALAEFL FDDEQALVRI DMSEYQERHA ISRLIGAPPG YVGYDEGGQL
TEAVRRRPYS VVLLDEIEKA HPDVFNILLQ VLDDGHLTDN KGRVVNFKNT IIIMTSNTGS
HLIQENFSHL TDENRDNVIA KTKDEVFELL QKSIRPEFLN RIDEFIMFTP LSRNEIGDIV
RMQFNRLQHQ LAEQSIFLSA TDEALDWLAQ LGYDPIYGAR PLKRVIQKRI LNELSKEILS
GKVTNDSVIQ LDTFDGQFVF LNKSE
//
