ID A0A5S9N3T1_9GAMM Unreviewed; 863 AA.
AC A0A5S9N3T1;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 27-MAR-2024, entry version 13.
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:CAA0084430.1};
GN ORFNames=OPDIPICF_00674 {ECO:0000313|EMBL:CAA0084430.1};
OS BD1-7 clade bacterium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae; BD1-7 clade.
OX NCBI_TaxID=2029982 {ECO:0000313|EMBL:CAA0084430.1, ECO:0000313|Proteomes:UP000441399};
RN [1] {ECO:0000313|EMBL:CAA0084430.1, ECO:0000313|Proteomes:UP000441399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB11_3 {ECO:0000313|EMBL:CAA0084430.1};
RA Holert J.;
RL Submitted (NOV-2019) 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; CACSIO010000001; CAA0084430.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5S9N3T1; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000441399; 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:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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 InterPro; IPR002078; Sigma_54_int.
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.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 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:UP000441399};
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 DOMAIN 576..814
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT COILED 414..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 863 AA; 96136 MW; F9C689104B89F636 CRC64;
MQYDRLTKTL QQALATAQSQ AMSAHNPSIE AEHFFQALLD DNTGYLINIL NRAQGDLPEL
KGAVKKVIDN LPTLGDASAG AEVRASGELM RLLTEADKLA TKKQDQYVAV EVFLLAIYET
SIGLKKLLES AGYKKPEIET IVEDIRGGES VSEQNSEENR QALDKYTIDL TERAEQGKLD
PVIGRDDEIR RTIQVLQRRT KNNPVIIGEP GVGKTAIVEG LAQRIINGEV PEGLKSKRLL
SLDLAGLIAG AKFRGEFEER LKALLKDLSK QEGQIILFID EIHTMVGAGK ADGAMDAGNM
LKPALARGEL HCVGATTLNE YREFIEKDAA LERRFQKVLV DEPSEEDTIA ILRGLKERYE
VHHGVDISDA AIIAATKLSM RYITDRNLPD KAIDLIDEAA SRIRMEIDSK PEALDKLERR
LIQLKIQREA VKKDKDESSK AQLDQLKEDI AEAEKAYADL EEVWKAEKSA LQGSQQIKAE
LEQARMDLEL ASRESNLSKM SELQYGVIPN LEKQLEEASK AEASGEKETN KLLRNRVTDE
EIAEIVSKWT GIPVTKMMEG DRDKLLRMED MLHKSVIGQG EAVKAVSSAV RRSRAGLSDP
NRPNGSFLFL GPTGVGKTEL CKSLSEFLFD TSEAMVRIDM SEYMEKHAVS RLIGAPPGYV
GYEEGGYLTE AVRRRPYSLI LLDEVEKAHP DVFNILLQVL DEGRLTDSQG RTVDFKNTVI
VMTSNLGSDM IQSLTGTASS DEIKDAVMEV VGKNFRPELL NRLDDVVYFH PLGKEHIRDI
ASIQLRHLQK RLADRELSLE VSDDAMHVII EQGYDPVYGA RPLKRAVQRL IEDPLATEIL
SGEFKSGDTV HIGCEDEKLI FTR
//
