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Database: UniProt
Entry: K9AL35_9STAP
LinkDB: K9AL35_9STAP
Original site: K9AL35_9STAP 
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
//
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