ID M5E4B6_9FIRM Unreviewed; 860 AA.
AC M5E4B6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=HSACCH_02593 {ECO:0000313|EMBL:CCU81111.1};
OS Halanaerobium saccharolyticum subsp. saccharolyticum DSM 6643.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC Halanaerobium.
OX NCBI_TaxID=1293054 {ECO:0000313|EMBL:CCU81111.1, ECO:0000313|Proteomes:UP000012063};
RN [1] {ECO:0000313|Proteomes:UP000012063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6643 {ECO:0000313|Proteomes:UP000012063};
RX PubMed=23640197; DOI=10.1128/genomea.00187-13;
RA Kivisto A., Larjo A., Ciranna A., Santala V., Roos C., Karp M.;
RT "Genome Sequence of Halanaerobium saccharolyticum subsp. saccharolyticum
RT Strain DSM 6643T, a Halophilic Hydrogen-Producing Bacterium.";
RL Genome Announc. 1:217-225(2013).
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:CCU81111.1}.
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DR EMBL; CAUI01000023; CCU81111.1; -; Genomic_DNA.
DR RefSeq; WP_005490437.1; NZ_CAUI01000023.1.
DR AlphaFoldDB; M5E4B6; -.
DR STRING; 1293054.HSACCH_02593; -.
DR eggNOG; COG0542; Bacteria.
DR InParanoid; M5E4B6; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000012063; 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 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000012063};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 7..105
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 407..575
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 860 AA; 98170 MW; 0F5B23F73E7014B4 CRC64;
MDMEKFTRKA QQSLVEAQNL AKDYQHQEIF PSHLFKALLN QDDGIVIPLL QKAEANIAEL
KAENEDLLQK LPQVYSEQGG QAYMSHQLNE IMREAEKQAE GLGDQYVSTE HFLLAILKNR
KTDLGKMLYQ KNLNYNDLKQ IIQEVRGGSK IDSQQGEEGF NVLEKYTIDI TELAKNGKLD
PVIGRDNLIR RVMQVLSRRR KNNPVLIGEP GVGKTAIVEG LAQRIINGDV PEGLKNKKVI
SLDMGSLVAG TKFRGEFEER LKSVLKEIKK AEGQIILFID EMHTLVGAGA TEGSMDAANL
LKPALARGEL HCVGATTLAE YKKHIEKDAA LERRFQPVQV SEPDIEDTVS ILRGLKEKYE
IHHGIKITDN AIVAAAKLSD RYLTERFLPD KAIDLIDEAA SKIRIEIDSM PIEIDELDRK
VRRLETEKEA LKNEDTEEAQ ERLKEIEEKL QELKDRRDPL RLKWKNEKDQ LAKMQELKEQ
IEQIEYRAEA AEREANYEEA ARLRYGKLNE LRKELAETSQ KVEESQQDAT HLVKEEVTEE
DIAEIVSLWT DIPLQKLMEE EKEKLIHLED ELEKRVVGQH DAVKAVSNAI RRSRTGLQDA
DQPLASFMFM GPTGVGKTEL AKTLAEYLFD DEKALTRIDM SEYMERHAVS KLIGSPPGYV
GFEEGGQLTE KVRRNPYSVI LFDEIEKAHP DVFNILLQIL DDGVLTDSQG KEVDFRNTVI
IMTSNVGSQY IQDLDDETKI KEEIDEALKG QFRPEFLNRI DEKIIFHSLT KADIFKIIDI
QISYLQDNLS EQDIEIDLSK AAKEELLELG FDPAYGARPL RRIIQNQIKD ELAMLILEEK
ITEGDQIKVD FEKGEFKFNK
//