ID A0A1B8PLW3_MORNO Unreviewed; 857 AA.
AC A0A1B8PLW3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=A9Z60_00110 {ECO:0000313|EMBL:OBX52137.1};
OS Moraxella nonliquefaciens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=478 {ECO:0000313|EMBL:OBX52137.1, ECO:0000313|Proteomes:UP000092671};
RN [1] {ECO:0000313|EMBL:OBX52137.1, ECO:0000313|Proteomes:UP000092671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 60284 {ECO:0000313|EMBL:OBX52137.1,
RC ECO:0000313|Proteomes:UP000092671};
RA Salva-Serra F., Engstrom-Jakobsson H., Thorell K., Gonzales-Siles L.,
RA Karlsson R., Boulund F., Engstrand L., Kristiansson E., Moore E.;
RT "Draft genome of Moraxella nonliquefaciens CCUG 60284.";
RL Submitted (JUN-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:OBX52137.1}.
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DR EMBL; LZDN01000001; OBX52137.1; -; Genomic_DNA.
DR RefSeq; WP_066890513.1; NZ_LZDN01000001.1.
DR AlphaFoldDB; A0A1B8PLW3; -.
DR OMA; SKMMQGE; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000092671; 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:UP000092671};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..143
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 409..489
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 857 AA; 95038 MW; 67CA060F31F71385 CRC64;
MNFDKLTRKV QTTLQNAQSL AVGRDNTAIF AIHILSVMLQ DESNVAMLSQ AGADINKLNH
DTTKKLGDLA TLSTPTGQAN LAPDLVQVLN LAEKFATDAG DSFVPSEWVL FALSQTGDTK
KVLTDAGVDA QKLQAIINHI RGGDTVKTQN AEDTRDALEK YTVNLTDRAK EGKLDPVIGR
DDEIRRTVQV LSRRTKNNPV LIGEPGVGKT AIVEGLAQRI VNGEVPESLK NKEVLSLDMG
SLIAGAKYHG EFEERLKGVL NDLAKQDGNI ILFIDELHTM VGAGKTSGAM DAGNMLKPAL
ARGELRCVGA TTLDEYRQYI EKDPALERRF QKVLVDEPSV EDTIAILRGL KERYELHHGV
RIMDAAIIAA AKMSHRYITD RQLPDKAIDL IDEAASRIKM ELDSKPESLD KLDRRIIQLK
MQLQTVKKED DAASQAQVKQ LQTQIDELEK EYNDLEEIWR AEKALVEGTK HAQIELDKAR
IALEKAQRDS NWEQAGRLQH EIIPNLQKQL ADEQYDDTNT PKLLRNKVTD NEIAEVVSHA
TGIPVAKMMQ GERDKMLGME RILHERVVGQ DEAVKSVANA VRRSRVGLSD PNRPSGSFLF
LGPTGVGKTE LTKSLANFLF DDETAMVRID MSEFMEKHSV SRLVGAPPGY VGYEEGGVLT
EAVRRKPYSV VLFDEVEKAH PDVFNVLLQV LDDGRLTDSQ GRVVNFKNTV IIMTSNLGSH
KIFDMAGDEY EEIKSAVMES VNAHFRPEFI NRIDEIVVFH PLGQSQMAGI ASIQLDRLRA
RLKERELSLV LSDEAINELV SVGYDPVFGA RPLKRAIVQE IENPLAQKLL SGEFIAGDTI
SVGVDNGVLT FDKLRFS
//