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Database: UniProt
Entry: G7Z3P3_AZOL4
LinkDB: G7Z3P3_AZOL4
Original site: G7Z3P3_AZOL4 
ID   G7Z3P3_AZOL4            Unreviewed;       867 AA.
AC   G7Z3P3;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB1 {ECO:0000313|EMBL:CBS88033.1};
GN   Synonyms=clpB {ECO:0000256|RuleBase:RU362034};
GN   OrderedLocusNames=AZOLI_2850 {ECO:0000313|EMBL:CBS88033.1};
OS   Azospirillum lipoferum (strain 4B).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS88033.1, ECO:0000313|Proteomes:UP000005667};
RN   [1] {ECO:0000313|Proteomes:UP000005667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RX   PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA   Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA   Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA   Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA   Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA   Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA   Zhulin I.B.;
RT   "Azospirillum genomes reveal transition of bacteria from aquatic to
RT   terrestrial environments.";
RL   PLoS Genet. 7:E1002430-E1002430(2011).
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   -!- 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|ARBA:ARBA00004496,
CC       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; FQ311868; CBS88033.1; -; Genomic_DNA.
DR   RefSeq; WP_014249012.1; NC_016622.1.
DR   AlphaFoldDB; G7Z3P3; -.
DR   STRING; 862719.AZOLI_2850; -.
DR   KEGG; ali:AZOLI_2850; -.
DR   HOGENOM; CLU_005070_4_2_5; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000005667; 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 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   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   COILED          414..494
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   867 AA;  95015 MW;  3966500E27EFEEF1 CRC64;
     MDFEQYTERS RGFVQAAQTL AVRRGHQRLT PEHLLKTLLD DKEGLAANLI RAAGGDPKAA
     LSAVDAELDK LPKVEGSGAG QLYLTPELSR VFEQAEKVAE KAGDSFVTAE RILLALAMAD
     GTPSARALKS AGVTPQALNT AINDIRKGRT ADSASAEQGY DALKKYARDL TAAARDGKLD
     PVIGRDEEIR RTIQVLARRT KNNPVLIGEP GVGKTAIVEG LAQRIVKGDV PEGLKNKQLL
     SLDLGALVAG AKYRGEFEER LKAVLSEIQA AAGEIVVFID ELHTLVGAGK SDGAMDASNM
     LKPALARGEL HCVGATTLDE FRKYIEKDAA LARRFQPVFV SEPTVEDTIS ILRGLKERYE
     VHHGVRITDS AIVSAATLSN RYITDRFLPD KAIDLIDEAA SRLRMAVDSK PEAIDELDRR
     IIQLKIEREA LKREQDAASR DRLVNLEREL SDLEQDSAEL TAKWQAEKDQ LQGAQKIKED
     LEKARTELET AQRDGNWGRA GELAYGVIPG LEKALKDAEA HASSRMLNEE VRDGDIAAVV
     SRWTGVPVDK MLAGEREKLL AMEDKLRGRV IGQDEAIVAV SNAVRRARAG LQDPNRPIGS
     FLFLGPTGVG KTELTKALAE FLFDDETAMV RLDMSEYMEK HSVARMIGAP PGYVGYEEGG
     ALTEAVRRRP YQVVLFDEVE KAHPDVFNVL LQVLDDGRLT DGQGRTVDFR NVVIIMTSNL
     GSQALAEQPE GEDSAAVREE VMEAVRAHFR PEFLNRLDEI LLFHRLDRRH MGGIVKIQLG
     RLTKMLADRE ITLTVDEAAT EWLAEAGYDP VYGARPLKRV IQRELQNPMA TLILEGRIKD
     GQTVAVGAEG GSLTIDGQPV SSLVRKG
//
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