ID Q7NR20_CHRVO Unreviewed; 875 AA.
AC Q7NR20;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE SubName: Full=Probable ClpA/B-type chaperone {ECO:0000313|EMBL:AAQ61627.2};
DE EC=3.4.21.92 {ECO:0000313|EMBL:AAQ61627.2};
GN OrderedLocusNames=CV_3965 {ECO:0000313|EMBL:AAQ61627.2};
OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS 12614 / NCIMB 9131 / NCTC 9757).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=243365 {ECO:0000313|EMBL:AAQ61627.2, ECO:0000313|Proteomes:UP000001424};
RN [1] {ECO:0000313|EMBL:AAQ61627.2, ECO:0000313|Proteomes:UP000001424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 /
RC NCTC 9757 {ECO:0000313|Proteomes:UP000001424};
RX PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA Vasconcelos A.T.R., de Almeida D.F., Almeida F.C., de Almeida L.G.P.,
RA de Almeida R., Goncalves J.A.A., Andrade E.M., Antonio R.V., Araripe J.,
RA de Araujo M.F.F., Filho S.A., Azevedo V., Batista A.J., Bataus L.A.M.,
RA Batista J.S., Belo A., vander Berg C., Blamey J., Bogo M., Bonato S.,
RA Bordignon J., Brito C.A., Brocchi M., Burity H.A., Camargo A.A.,
RA Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B.,
RA Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Pasa T.B.C., Duran N.,
RA Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S.,
RA Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A.,
RA Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA Grattapaglia D., Grisard E.C., Guimaraes C.T., Hanna E.S., Hungria M.,
RA Jardim S.N., Laurino J., Leoi L.C.T., Fassarella L., Lima A.,
RA Loureiro M.F., Lyra M.C.P., Macedo M., Madeira H.M.F., Manfio G.P.,
RA Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B.,
RA Meissner R.D.V., Menck C.F.M., Moreira M.A.M., Nascimento F.F.,
RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA Pedrosa F.O., Pena S.J.D., Perreira J.O., Perreira M., Pinto L.S.R.C.,
RA Pinto L.S., Porto J.I.R., Potrich D.P., Neto C.E.R., Reis A.M.M.,
RA Rigo L.U., Rondinelli E., dos Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT "The complete genome sequence of Chromobacterium violaceum reveals
RT remarkable and exploitable bacterial adaptability.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
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. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK.
CC {ECO:0000256|ARBA:ARBA00025613}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675}.
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DR EMBL; AE016825; AAQ61627.2; -; Genomic_DNA.
DR AlphaFoldDB; Q7NR20; -.
DR STRING; 243365.CV_3965; -.
DR KEGG; cvi:CV_3965; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_1_2_4; -.
DR Proteomes; UP000001424; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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; IPR017729; ATPase_T6SS_ClpV1.
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; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR03345; VI_ClpV1; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF184; ATPASE WITH CHAPERONE ACTIVITY-RELATED; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 1.
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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:AAQ61627.2};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001424};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 5..158
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 152..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 436..503
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 875 AA; 94648 MW; 7B48DFEA4EF3B14B CRC64;
MKSLIDRLTP TARQAIEQAA SRALARTHFE IEIEHVLLAM FDQDDNAALA ALRALGADLG
RVERELDAAL DNFRSGNTRN PVLSSWLPKW LEKAWLLASA EHGQDSVSTL DLLLALWQDD
ALRGALQSGA PALARQDAGR LSGAYAALRQ HGGEAAGGEQ PSAAADEGEG EAPAAPQGKR
GGAALDKYTI DLTAQAKAGK IDPILGRDVE IRQMIDILMR RRQNNPILTG EPGVGKTAVV
EGLARKIVLG EVPPVLSGVT LRTLDLGLLQ AGASVKGEFE NRLRQVIDEV KASPVPIILF
IDEAHTLIGA GGAAGQNDAA NLLKPALARG ELRTIAATTW AEYKKYFEKD AALARRFQVV
KVEEPAPEIA VQMVRGLTDA MAKHHKVEIL NEAVAAAVQL SSRYIAGRQL PDKAISVLDT
ACARVALSRA GKPGPIEDVT VLIDNIDRET AALEREEGHA ERIAELQAQR AKLEQDLAAL
HQAWEAQQKL IEEIDELKAA KDEAKPAKGR KLSPLQAKRK ELRELQKHQP LAFECVDESV
IADVIAGWTG IPLGRMVSNE LEQVQKLAKL LAERVIGQDH ALEQIAERVQ IAKANLEDPG
KPKGVFLLVG PSGVGKTETA LALAEALYGG ERNLITINMS EYQEAHSVSG LKGSPPGYVG
YGEGGVLTEA VRRKPYSVVL LDEVEKAHPD VLELFFQVFD KGVLEDSEGR EVDFKNTIIL
LTSNAGTDLV MRACEHGVTV EDETRDPTAE DLVEILRPTL QKTFKPAFLG RLTIVPYFPI
SDDVLRAIVG LKLDKIRRRI ADNHGAQVEF PEELADQMAA RCLDVDSGAR NADAILTRTL
LAQISNDLLS RMASGKPVKK IAVALKGEQV KVKVS
//
