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Database: UniProt
Entry: A0A1H3WW12_9BACT
LinkDB: A0A1H3WW12_9BACT
Original site: A0A1H3WW12_9BACT 
ID   A0A1H3WW12_9BACT        Unreviewed;       870 AA.
AC   A0A1H3WW12;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN05192529_10440 {ECO:0000313|EMBL:SDZ91313.1};
OS   Arachidicoccus rhizosphaerae.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Arachidicoccus.
OX   NCBI_TaxID=551991 {ECO:0000313|EMBL:SDZ91313.1, ECO:0000313|Proteomes:UP000199041};
RN   [1] {ECO:0000313|EMBL:SDZ91313.1, ECO:0000313|Proteomes:UP000199041}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Vu-144 {ECO:0000313|EMBL:SDZ91313.1,
RC   ECO:0000313|Proteomes:UP000199041};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
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DR   EMBL; FNQY01000004; SDZ91313.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3WW12; -.
DR   STRING; 551991.SAMN05192529_10440; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000199041; 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 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   Hydrolase {ECO:0000313|EMBL:SDZ91313.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SDZ91313.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199041};
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          399..524
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   870 AA;  97672 MW;  C05A56973374B5CD CRC64;
     MNPNNYTIKA QELIQAAQQI AYNNGDLNIE TNHLLLALLG EKESAIEFLL KKNDVNIAYT
     EQKIRDSLSR LPKAASGEPA QQVGREMNNT LLRAAKDISQ FGDEFINPEH LLLALVQGSD
     DTAKILKDAG LTQKGLVAAI KDLRQGAGSV NSQTANQEVG SLKKYAKNLN ELAQAGKLDP
     VIGRDEEIRR TLHILSRRSK NNPILVGEPG VGKTAIVEGL AHRIINGDVP ENLKSKIIYS
     LDMGLLIAGA KYKGEFEERL KGVIKDVATS DGEIILFIDE IHTLVGAGGG EGAMDAANIL
     KPALARGDLR AIGATTLNEY QKFFEKDKAL ERRFQKVMVD EPTIEDAVSI LRGLKERYET
     HHHVLIRDEA IIAAVELSNR YITDRFLPDK AIDLIDESAA KLRLEMNSMP EELDELERKI
     RQLEIEREAI KRENDQAKLK ELNTNIGNLM VERDTYKAKW QQEKEVVEKM QNAKAAIDSL
     KLEAEKAERE GDYGKVAEIR YGKIKEQQEI IDQTNHELQD ISEKRLLKEE VDAEDIAENV
     AKATGIPVSR MLQSEKDKLL HLEDHLHQRV VGQQEAITAV SDAIRRSRAG LGDPKRPIGS
     FIFLGTTGVG KTELAKALAE FLFDDESMMT RIDMSEYQEK HSVSRLVGAP PGYVGYEEGG
     QLTEAVRRKP YSVVLFDEIE KAHPDVFNIL LQVLDDGHLT DNKGRTVNFK NTIIIMTSNI
     GSHLIMDAFE NHQDDIDKAE QVAKDEVMNL LKETIRPEFL NRIDEIVMFH PLLKKEIKNI
     INIQLRQLKR QIAQGGIHID FSDYVMDYLS ENGYDIQFGA RPLKRFIQKA IVNPLSKKIL
     AGEIDRDHPV LVDVFDGIVV FRNEEQVASK
//
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