ID A0A177R8P9_9BACT Unreviewed; 854 AA.
AC A0A177R8P9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=AYO49_00940 {ECO:0000313|EMBL:OAI56201.1};
OS Verrucomicrobiaceae bacterium SCGC AG-212-N21.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Verrucomicrobiaceae.
OX NCBI_TaxID=1799659 {ECO:0000313|EMBL:OAI56201.1, ECO:0000313|Proteomes:UP000077910};
RN [1] {ECO:0000313|Proteomes:UP000077910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC AG-212-N21 {ECO:0000313|Proteomes:UP000077910};
RA Choi J., Stepanauskas R., Howe A.;
RL Submitted (FEB-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}.
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:OAI56201.1}.
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DR EMBL; LSTJ01000122; OAI56201.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177R8P9; -.
DR Proteomes; UP000077910; 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:UP000077910};
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; 95144 MW; B9D09F271CE4AA06 CRC64;
MNPDRTTVKM QEALAGGQSI AGRYGHAEIK PSHVFLALLD QSEGVTRPLL EKVGANVSSL
KSAVEAHLAR QPKVSGGGGP QYLSSDLRET LTNAEKEQRA LKDEFLSVEH FLLALAKTRT
DIESILKQAG LKHGTMLQAL TSVRGAQRVT DQDPEGKYQT LEKYGTDLTA RAKQGKIDPV
IGRDEEIRRV MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA RRIVAGDVPD SLKNKRLISM
DLGGMMAGAK FRGEFEERLK AFLKEVTSSE GEIILFIDEL HTIVGAGKAE GAMDAGNLLK
PQLARGELRC VGATTLDEYR KHIEKDPALE RRFQPVLVGE PSVEDTIAIL RGLKERYEVH
HGVRIQDNAI IAAATLSHRY ISDRFLPDKA IDLVDEAASR IKIELDSMPT EIDVIEREIM
QDEMERQVLK KEKDAASITR LEKLEKDIAA LKEKSSALKL QWQKEKESVD ASRKVMEEID
RLRTEQEQAQ RRGDFGRAGE IQYGLIPDLE KKLAAASAAQ TSSQLLREEV TEEDIAKVVA
SWTGIPVSRL QEGERSKLSH MEDRLGLRVI GQKNAIKAVS NAVRRARAGL QDENRPIGSF
LFLGPTGVGK TELSKALAEF LFDDENAMTR IDMSEYMEKH SVARLIGAPP GYVGYEEGGQ
LTEAVRRRPY SVVLFDEVEK AHPDVFNTLL QVLDDGRITD GQGRTVDFRN TVLIMTSNIG
SQAIQEVANA EQREAMVRDA LKKFFRPEFL NRIDEVITFD RLDARDLDAI VKIQVQRVVD
RMRKHNITLK ISDEAVRKVA DEGYDPVYGA RPLKRAIQRL ILDPLSLEML EGKFRDGDVI
EGRLENGAIV FDKH
//
