ID K6XTV2_9ALTE Unreviewed; 858 AA.
AC K6XTV2;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:GAC24049.1};
GN ORFNames=GMES_1753 {ECO:0000313|EMBL:GAC24049.1};
OS Paraglaciecola mesophila KMM 241.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1128912 {ECO:0000313|EMBL:GAC24049.1, ECO:0000313|Proteomes:UP000006263};
RN [1] {ECO:0000313|EMBL:GAC24049.1, ECO:0000313|Proteomes:UP000006263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMM 241 {ECO:0000313|EMBL:GAC24049.1,
RC ECO:0000313|Proteomes:UP000006263};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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:GAC24049.1}.
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DR EMBL; BAEP01000032; GAC24049.1; -; Genomic_DNA.
DR RefSeq; WP_006992200.1; NZ_BAEP01000032.1.
DR AlphaFoldDB; K6XTV2; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000006263; 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:GAC24049.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:GAC24049.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006263};
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 858 AA; 95494 MW; 7DAEB86F60147ADC CRC64;
MRLDSFTSKF QLAISDAQSI ALGRDHQYIE PVHLMTALLN QQGGSVRSLF DHAKVNVNTL
RSALAEAVDH LPRVEGVGGD VQLAKETVVL LNLSDKIAQK RKDKYITSEI FVLAAVQDKG
KLGELLRQIG ASEESIDKAI EAMRGGQTVN DPNAEDVRQA LEKFTTDLTE RAEQGKLDPV
IGRDDEIRRT IQVLQRRTKN NPVLIGQPGV GKTAIAEGLA QRIINSEVPE GLKNKRVLSL
DMGALIAGAK FRGEFEERLK AVLNELAKEE GRVILFIDEL HTMVGAGKGE GAMDAGNMLK
PALARGELHC VGATTLDEYR QFIEKDAALE RRFQKVLVDE PSVEDTVAIL RGLKERYELH
HSVEITDPAI VAAASLSHRY ISDRQLPDKA IDLIDEAASS IRMQMDSKPE DMDRLERRII
QLKLEEQALA KEKDEASHKR LELIEIEREQ AEIKFSELEK IWKSEKQAMQ GTQNIRAELD
QAKLDLEIAR RASDLSRMSE LQYGRIPELE SKLELATESE SQPLEHQLLK NRVTESEIAD
VLSRWTGIPV SKMLEGEKDK LMSMETALHE RVVGQSEAVN AVSNAIRRSR AGLADPNKPI
GSFLFLGPTG VGKTELCKTL ANFLFDTEDA MVRIDMSEFM EKHSVSRLVG APPGYVGYEE
GGYLTEAVRR KPYSVILLDE IEKAHPDVFN ILLQVLDDGR LTDGQGRTVD FKNSVIIMTS
NLGSDIIQEQ HSENDYEKMK QSVLNVLSTH FRPEFLNRVD ETVVFHPLGL AQITSIASKQ
LQFLRNRLEE KGIGLELTDA ALKKIAEAGF DPVYGARPLK RAIQMEIENP LAQKILSGKL
VSEGVVSIDA DENGLIID
//
