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Database: UniProt
Entry: A0A1Q2SLJ1_9GAMM
LinkDB: A0A1Q2SLJ1_9GAMM
Original site: A0A1Q2SLJ1_9GAMM 
ID   A0A1Q2SLJ1_9GAMM        Unreviewed;       857 AA.
AC   A0A1Q2SLJ1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=TAO_0628 {ECO:0000313|EMBL:BAW79998.1};
OS   Candidatus Nitrosoglobus terrae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Candidatus Nitrosoglobus.
OX   NCBI_TaxID=1630141 {ECO:0000313|EMBL:BAW79998.1, ECO:0000313|Proteomes:UP000243679};
RN   [1] {ECO:0000313|EMBL:BAW79998.1, ECO:0000313|Proteomes:UP000243679}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAO100 {ECO:0000313|EMBL:BAW79998.1,
RC   ECO:0000313|Proteomes:UP000243679};
RX   PubMed=28072419; DOI=10.1038/ismej.2016.191;
RA   Hayatsu M., Tago K., Uchiyama I., Toyoda A., Wang Y., Shimomura Y.,
RA   Okubo T., Kurisu F., Hirono Y., Nonaka K., Akiyama H., Itoh T., Takami H.;
RT   "An acid-tolerant ammonia-oxidizing ?-proteobacterium from soil.";
RL   ISME J. 11:1130-1141(2017).
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; AP014836; BAW79998.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q2SLJ1; -.
DR   KEGG; ntt:TAO_0628; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000243679; 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   Reference proteome {ECO:0000313|Proteomes:UP000243679};
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   857 AA;  96338 MW;  78E89739205B03B1 CRC64;
     MRQDRFTTKF QEALADAQSL ALRHDHQFLE PLHVMLTLLD QQGGTVLPLL MRAGVDGNYL
     HAQLNNALKQ LPQIQGTPGE IHLSQELARL LNITDKLAHQ RQDQYISSEL FLLAAVEDKG
     QLGELLRKNK VSKANIEAAI NAMRGGQQIN DPGAEDQRQA LERYTVDLTQ RAEQGKLDPV
     IGRDDEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIAEGLA QRIINGEVPE GLKHRRLLAL
     DMGALIAGAK FRGEFEERLK AVLKDVSKAE GNIILFIDEL HTMVGAGKAE GAMDAGNMLK
     PALARGELHC IGATTLDEYR QYIEKDAALE RRFQKVLVDE PNVEDTIAIL RGLNERYEVH
     HGVEITDPAI VAAVSLSHRY ITDRKLPDKA IDLIDEAASH IRMEIDSKPE PMDRLERRII
     QLKIEREALR KETDEASKKR LEILETELNT LEKEYADLEE IWKAEKATLS GAQGIKEKLE
     QARLDLDSAR RAGDLARMSE LQYGRIPELQ KQLDAAAAIE SHDFKLLRNK VTEEEIAGVV
     SKWTGIPVSK MLEGERDKLL KMEEALQQRV VGQMEAITTV SNAIRRSRAG LSDPYRPNGS
     FLFLGPTGVG KTELCKALAV FLFDTQEAMI RIDMSEFMEK HAVARLIGAP PGYVGFEEGG
     YLTEAVRRKP YSVILLDEVE KAHPDVFNLL LQVLDDGRLT DSHGRTVDFR NTIVVMTSNL
     GSQIIQEMIG EDDYPRMKKA VMEIVSQHFR PEFINRVDDV VVFHPLLKEQ LHAIAKIQIA
     YLQRRLAAQD MQLSVTDIAL DKITEVGFDP VYGARPLKRA IQQQLENPIA QEILKGTFKS
     GHLIKVGFKE DRFVFER
//
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