ID A0A177NEJ9_9GAMM Unreviewed; 857 AA.
AC A0A177NEJ9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=A1359_07510 {ECO:0000313|EMBL:OAI16488.1};
OS Methylomonas lenta.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=980561 {ECO:0000313|EMBL:OAI16488.1, ECO:0000313|Proteomes:UP000078476};
RN [1] {ECO:0000313|EMBL:OAI16488.1, ECO:0000313|Proteomes:UP000078476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-45370 {ECO:0000313|EMBL:OAI16488.1,
RC ECO:0000313|Proteomes:UP000078476};
RA Ploux O.;
RL Submitted (MAR-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:OAI16488.1}.
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DR EMBL; LUUI01000095; OAI16488.1; -; Genomic_DNA.
DR RefSeq; WP_066981016.1; NZ_LUUI01000095.1.
DR AlphaFoldDB; A0A177NEJ9; -.
DR STRING; 980561.A1359_07510; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000078476; 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:UP000078476};
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; 95579 MW; E5D48D46C971C9CE CRC64;
MRMDKLTSKF QQALGEAQSL ALGKDHQFIE PLHVMLALLD QEGGSVKPLL QQVGVQVNAL
HKDLNKDIDS LASVSGSGGD VQLSNELSRI LNLTDKLAQK RKDAFISSEL FLLAALETSG
TLQNILKRAG VTASAVEKAI DNMRGGQNVN DANAEDQRQA LKKYTINLTE RAEQGKLDPV
IGRDDEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIINGEVPE GIKGKQLLSL
DMAALIAGAK FRGEFEERLK AVLNDLAKME GQVILFIDEL HTMVGAGKAE GAMDAGNMLK
PALARGELHC VGATTLDEYR KYIEKDAALE RRFQKVLVDE PNVEDTIAIL RGLKERYEIH
HRVDITDPAI VAAAVLSHRY IADRQLPDKA IDLIDEAASR IRMEIDSKPE EMDRLLRRLI
QLRMEKESLR KEKDDASRKR LEQVQEQIDE ADKEYSDLDE IWKAEKAALQ GTASIKESLE
HARLELEAAR RNQDYTRMSE LQYGDIPKLE KELDLASQAE MQETTLLRSK VTEEEIAEVV
SKWTGIPVSK MMQGEREKLL QMEENLSKRV IGQTEALKAV SNAIRRSRAG LSDPNRPNGS
FLFLGPTGVG KTELCKALAE FMFDTEEAMV RIDMSEFMEK HSVARLIGAP PGYVGYEEGG
YLTEAVRRKP YSVILLDEIE KAHADVFNVL LQVLDDGRLT DGQGRTVDFR NTVIVMTSNL
GSSVIQELSG EENYTTMKDA VMEIVGQHFR PEFINRVDEA VVFHPLGQGQ IRAICSIQID
QLRRRLQEKD MELELSETAL DLLGEAGFDP VYGARPLKRA IQRQLENPLA NEILSGHFLP
GDIIKVDNAT DGLTFSK
//