ID A0A327Y972_9BACI Unreviewed; 866 AA.
AC A0A327Y972;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=B0I26_11431 {ECO:0000313|EMBL:RAK17027.1};
OS Anoxybacillus vitaminiphilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=581036 {ECO:0000313|EMBL:RAK17027.1, ECO:0000313|Proteomes:UP000248555};
RN [1] {ECO:0000313|EMBL:RAK17027.1, ECO:0000313|Proteomes:UP000248555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8979 {ECO:0000313|EMBL:RAK17027.1,
RC ECO:0000313|Proteomes:UP000248555};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUN-2018) 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:RAK17027.1}.
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DR EMBL; QLMH01000014; RAK17027.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A327Y972; -.
DR Proteomes; UP000248555; 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 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 Hydrolase {ECO:0000313|EMBL:RAK17027.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RAK17027.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 1..149
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 85..112
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 415..536
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 866 AA; 98725 MW; 7EEA5AB00470449B CRC64;
MNKMTEKVQE AFMSAQSLAM QHYHQEIDIV HLLLALIEQQ DGLARRIFDY LHIDIEAFVN
DLHALIKKKP QVIGAGVEKG KVYITHHLQR LLVNAEEEAK RLQDEYISVE HLLLALTNDT
QANEIVSLFK KYRIERHSLL KVLMDIRGNQ RVTSATPEAT YEVLKKYGRD LVAEVKAGKI
DPVIGRDSEI RRVIRILSRK TKNNPVLIGE PGVGKTAIVE GLAQRIVRKD VPEGLKDKTI
FALDMSSLVA GAKFRGEFEE RLKAVLNEIK KSEGRIILFI DELHTIVGAG RAEGAMDAGN
MLKPMLARGE LHCIGATTLD EYRQYIEKDP ALERRFQQVL VEEPTVEDTI SILRGLKERF
EIHHGVNIHD RALVAAATLS DRYISERFLP DKAIDLVDEA CAMIRTEIDS MPTELDEVMR
RVMQLEIEEA ALRKETDEAS KERLEALTKE LADLREKANS MKVKWQQEKE EIQNVRNLRE
ALEKAKRELE EAENEYDLNK AAELRHGRIP QLEKELKQLE QKMSEKQEEG RLLREEVTEE
EIAEVVSRWT GIPLAKLVEG EREKLLRLQD ILHERVIGQD EAVELVADAV LRARAGIKDP
NRPIGSFIFL GPTGVGKTEL AKALAQSLFD SEEQMVRIDM SEYMEKHAVS RLIGAPPGYV
GYEEGGQLTE AVRRKPYSVI LLDEIEKAHP EVFNILLQVL DDGRITDSQG RTVDFKNTVI
IMTSNIGSHF LLEGVTNEGE MKEETREQVL QQLRAHFRPE FLNRIDDIIL FKPLTVNEVK
GIVDKLVKEL SQRLADRHIT LTLTDKAKEY IATAGFDPVY GARPLRRFIQ KHIETKLAKE
IIAGRIKDYS NVLIDYENGQ IMLEKQ
//
