ID Q1MS43_LAWIP Unreviewed; 877 AA.
AC Q1MS43;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:CAJ54182.1};
GN OrderedLocusNames=LI0126 {ECO:0000313|EMBL:CAJ54182.1};
OS Lawsonia intracellularis (strain PHE/MN1-00).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Lawsonia.
OX NCBI_TaxID=363253 {ECO:0000313|EMBL:CAJ54182.1, ECO:0000313|Proteomes:UP000002430};
RN [1] {ECO:0000313|EMBL:CAJ54182.1, ECO:0000313|Proteomes:UP000002430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHE/MN1-00 {ECO:0000313|EMBL:CAJ54182.1,
RC ECO:0000313|Proteomes:UP000002430};
RA Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT "The complete genome sequence of Lawsonia intracellularis: the causative
RT agent of proliferative enteropathy.";
RL Submitted (NOV-2005) 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; AM180252; CAJ54182.1; -; Genomic_DNA.
DR RefSeq; WP_011526209.1; NC_008011.1.
DR AlphaFoldDB; Q1MS43; -.
DR STRING; 363253.LI0126; -.
DR KEGG; lip:LI0126; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_7; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000002430; Chromosome.
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:UP000002430};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..151
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 410..497
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 877 AA; 98504 MW; 36EEBF6B49D2D083 CRC64;
MDVNKLTQKS QEALSEAQRL SAQYGHQEVD VEHLALALTI QENGFVPRVL EQAKVHVKVV
ISALEEVLKK RPSVRGPGSE MGKITISQRL SKVIANAELL AKRLGDEYVS VEHLFAECLN
EPESTGMGQV AKEIHLTSQR FIEVMLAVRG PHRVTSPTPE DSYEALKKYG RDLVEAARKG
KLDPVIGRDA EIRRVIRILS RRTKNNPVLI GEAGVGKTAI VEGLAFRIVQ GDVPEGLKDK
SIFALDMGSL IAGAKYRGEF EERLKAVLTE VEKSEGRIVL FIDELHTIVG AGKADGAMDA
GNFLKPMLAR GELHCIGATT LDEYRKYIEK DPALERRFQP VMVDEPSVQD TISILRGLKE
RFEVHHGVRI SDSAIVEAVV LSDRYISDRQ LPDKAIDLID EAAAMIRTEI DSLPSELDEV
NRKIMQLEIE REALRKESDS ASHERLVRLE EELKVLQSTQ SELKKQWETE KGSIDSLRNI
KEQIEQTRLA IDEATRNGEL SKAAELKYSK LFELEKQLEE RESKADGPRL LKEEVRPDDV
ANIVARWTGI PVTRLLESEK EKLLRLPDTL HERVIGQDEA VNVICNAVLR TRAGLSDPKR
PQGSFIFLGP TGVGKTELCK ALAESLFDTE ENMVRFDMSE YMEKHSVARL IGAHPGYVGY
EEGGQLTNAV KRKPYSVILF DEVEKAHPDV FNIFLQLLDD GRLTDNAGRT INFRNTIIIM
TSNIGAYKLL EGISPDGSFH EGVYESVMGD LKQHFRPEFL NRVDDVVLFK PLLADQISSI
IDLQLRSLKK RLESQKVTLE LTHSAHLYLA ENGYDPHYGA RPLKRYLQRV VETPLAKMII
SGKVHENQQI VIDYSESDSS LQYGVKSASE DINWVQV
//
