ID K9AL35_9STAP Unreviewed; 865 AA.
AC K9AL35;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=C273_06423 {ECO:0000313|EMBL:EKU48073.1};
OS Staphylococcus massiliensis S46.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1229783 {ECO:0000313|EMBL:EKU48073.1, ECO:0000313|Proteomes:UP000009885};
RN [1] {ECO:0000313|EMBL:EKU48073.1, ECO:0000313|Proteomes:UP000009885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S46 {ECO:0000313|EMBL:EKU48073.1,
RC ECO:0000313|Proteomes:UP000009885};
RX PubMed=23929469;
RA Srivastav R., Singh A., Jangir P.K., Kumari C., Muduli S., Sharma R.;
RT "Genome Sequence of Staphylococcus massiliensis Strain S46, Isolated from
RT the Surface of Healthy Human Skin.";
RL Genome Announc. 1:e00553-13(2013).
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:EKU48073.1}.
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DR EMBL; AMSQ01000008; EKU48073.1; -; Genomic_DNA.
DR RefSeq; WP_009383501.1; NZ_AMSQ01000008.1.
DR AlphaFoldDB; K9AL35; -.
DR STRING; 1229783.C273_06423; -.
DR PATRIC; fig|1229783.3.peg.1298; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000009885; 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:UP000009885};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251};
KW Stress response {ECO:0000256|ARBA:ARBA00023016,
KW ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 411..532
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 865 AA; 98158 MW; C59D3E174612AEFD CRC64;
MDINQMTHAV QGALQKAIEE AKNQKIQNVE IECVLKSCVL EHDSLFKSIL ERAKVDTDEL
IEAYNKKLAS YATVKGDNVT YGEYVGPKTN ELFTKSKQYM EQYEDAYISM EHVLLAAMEI
DQTTQSFVSH KEKVIKEIIK KIRGGNHVTS QNPEVNYEAL EKYGRDLVEE VRNGKMDPVI
GRDDEIRNAI RILSRKTKNN PVLIGEPGVG KTAIVEGIAQ RIVRKDVPET LMDKTVFELD
LSALVAGAKY RGEFEERLKA VLKEIKESEG RILLFIDEIH MLVGAGKTDG AMDAGNMLKP
MLARGELHCI GATTLNEYRE YIEKDSALER RFQKVNVSEP DIEDTISILR GLKERYEVYH
GVRIQDRALV AAAELSDRYI TDRFLPDKAI DLVDQACATI KTEMGSNPTE LDQVNRRVMQ
LEIEESALKN ESDQSSQNRL KELQEELANE KEKQAEISSR VEKEKEKIKV VQEKRTELDE
RRKALEDAEN NYNLEKAAEL QHGKIPQLER ELKELEEQFQ EADGNKNDHI IREMVSDEEI
GDIVSQWTGI PVSKLVETER EKLLNLSDIL HERVVGQDKA VDLVSDAVVR ARAGIKDPNR
PIGSFLFLGP TGVGKTELAK SLASTLFDSE KHMIRIDMSE YMEKHAVSRL IGAPPGYVGH
DEGGQLTEAV RRNPYSVILL DEIEKAHSDV FNVLLQILDD GRLTDSKGRS VDFKNTIIIM
TSNIGSDILL DNVQSTGDIQ ESTEKSVMSR LHDYFKPEIL NRMDDIVLFK PLTVEDMEMI
IDRIITNLNI RLMDQGIQLD VSKEAKVWMG RTAYEPQFGA RPLKRFVQKH IETPIARLMI
KENFDEGTTI KVSLEDESLN FEVES
//