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Database: UniProt
Entry: A0A1E3GQA1_9GAMM
LinkDB: A0A1E3GQA1_9GAMM
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ID   A0A1E3GQA1_9GAMM        Unreviewed;       861 AA.
AC   A0A1E3GQA1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
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:ODN66233.1};
GN   ORFNames=A9E74_02039 {ECO:0000313|EMBL:ODN66233.1};
OS   Methylophaga muralis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Methylophaga.
OX   NCBI_TaxID=291169 {ECO:0000313|EMBL:ODN66233.1, ECO:0000313|Proteomes:UP000094379};
RN   [1] {ECO:0000313|EMBL:ODN66233.1, ECO:0000313|Proteomes:UP000094379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bur 1 {ECO:0000313|EMBL:ODN66233.1,
RC   ECO:0000313|Proteomes:UP000094379};
RA   Vasilenko O.V., Doronina N.V., Shmareva M.N., Tarlachkov S.V.,
RA   Mustakhimov I., Trotsenko Y.A.;
RT   "Draft Genome Sequence of Methylophaga muralis Bur 1.";
RL   Submitted (JUL-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ODN66233.1}.
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DR   EMBL; MCRI01000024; ODN66233.1; -; Genomic_DNA.
DR   RefSeq; WP_069296458.1; NZ_MCRI01000024.1.
DR   AlphaFoldDB; A0A1E3GQA1; -.
DR   STRING; 291169.A9E74_02039; -.
DR   PATRIC; fig|291169.3.peg.2049; -.
DR   Proteomes; UP000094379; 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: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:UP000094379};
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   861 AA;  96031 MW;  8A9C6EEA98C425CD CRC64;
     MQADKFTSKF QDALGAAQSL AVGRDHQIIE PAHLLLALLN QQGGTVKPLL AQSGVNVPAY
     QADLEAQLNR FPQVEGGNGD IRISADLSRL LNQTDKLAQQ RQDQFISSEL LILAAVEDKN
     QTGELLRKHG ANKTNINNVI EKIRGGERVT DQNAEEQRQA LEKYTIDLTA RAESGKLDPV
     IGRDDEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE GMKNKRVLAL
     DMGSLIAGAK FRGEFEERLK AVLNDLSKQE GQIILFIDEI HTMVGAGKAE GAMDAGNMLK
     PALARGELHC IGATTLDEYR QYVEKDAALE RRFQKVLVGE PSVESTIAIL RGLSERYEVH
     HGVEITDPAI VAAANLSHRY ITDRNLPDKA IDLIDEAASR IRMEIDSKPE VLDRLERRLI
     QLKIERVALQ KESDEASKKR LDTLETEMKK LAREYTDLEE VWKSEKAALH GSQHIKEELE
     KARLELESAN RSGNLEKMSE LQYGRIPALE KQYDLATQAE MQEFTLLRNK VGEEEIAEVV
     SKWTGIPVSK MLEGERDKLL KMDEALHQRV IGQDEAVNSV ANAIRRSRAG LSDPNRPNGS
     FLFLGPTGVG KTELCKSLAT FLFDTEEAMV RIDMSEFMEK HSVARLVGAP PGYVGYEEGG
     YLTEAVRRKP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVIVMTSNL
     GSSIIQEMAG EDNYEAMKNA VMEIVGQHFR PEFINRVDDV VVFHPLQKSQ IRAIADIQLE
     HLRQRLAEKE MGLELSDAAL DMLSEAGFDP VYGARPLKRV IQHQLENPLA QALLSGRFVA
     GHVIKVDVQD EDLVFTSELR H
//
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