(data stored in ACNUC7421 zone)

SWISSPROT: C7QHA1_CATAD

ID   C7QHA1_CATAD            Unreviewed;       872 AA.
AC   C7QHA1;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   05-JUL-2017, entry version 67.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   OrderedLocusNames=Caci_0085 {ECO:0000313|EMBL:ACU69040.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69040.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69040.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
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.
CC       {ECO:0000256|RuleBase:RU362034}.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|SAAS:SAAS00721915}.
CC   -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC       {ECO:0000256|RuleBase:RU362034}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034,
CC       ECO:0000256|SAAS:SAAS00738470}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432, ECO:0000256|SAAS:SAAS00548741}.
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DR   EMBL; CP001700; ACU69040.1; -; Genomic_DNA.
DR   RefSeq; WP_012784335.1; NC_013131.1.
DR   STRING; 479433.Caci_0085; -.
DR   PRIDE; C7QHA1; -.
DR   EnsemblBacteria; ACU69040; ACU69040; Caci_0085.
DR   KEGG; cai:Caci_0085; -.
DR   eggNOG; ENOG4105C2Z; Bacteria.
DR   eggNOG; COG0542; LUCA.
DR   HOGENOM; HOG000218211; -.
DR   KO; K03695; -.
DR   OMA; HHKVRIK; -.
DR   OrthoDB; POG091H019M; -.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016485; P:protein processing; IEA:UniProtKB-UniRule.
DR   GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1780.10; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR017730; Chaperonin_ClpB.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004176; Clp_N.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 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; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF81923; SSF81923; 1.
DR   TIGRFAMs; TIGR03346; chaperone_ClpB; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C7QHA1.
DR   SWISS-2DPAGE; C7QHA1.
KW   ATP-binding {ECO:0000256|RuleBase:RU004432,
KW   ECO:0000256|SAAS:SAAS00433968};
KW   Chaperone {ECO:0000256|RuleBase:RU004432,
KW   ECO:0000256|SAAS:SAAS00480820};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Cytoplasm {ECO:0000256|RuleBase:RU362034,
KW   ECO:0000256|SAAS:SAAS00738398};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU004432,
KW   ECO:0000256|SAAS:SAAS00433972};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW   Repeat {ECO:0000256|SAAS:SAAS00721905};
KW   Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN      199    346       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      602    755       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      776    867       ClpB_D2-small. {ECO:0000259|SMART:
FT                                SM01086}.
SQ   SEQUENCE   872 AA;  94855 MW;  F9F22AA5B63F0239 CRC64;
     MDSQKLTTKS QEALSVAIRE ATRAGNPQVE SIQVLLALLG QVEGTTRPLL EAVGVDRAAL
     SQAVTAAAER LPSASGSTVS APTLARNTLN ALNAAGDEAR KLDDEYVSTE HLLLGLALGN
     DSTADLLKKA GATPQALREA FGKVRGSARV TSQDPEATYQ ALEKYGVDLT AAARDGKLDP
     VIGRDAEIRR VVQVLSRRTK NNPVLIGEPG VGKTAVVEGL AQRIIAGDVP ESLRDKRLVS
     LDLGAMVAGA KYRGEFEERL KAVLADIKDS EGQIVTFIDE LHTVVGAGAT GDSSMDAGNM
     LKPMLARGEL RMVGATTLDE YRERIEKDPA LERRFQQVLV DEPTVEDTIA ILRGLKGRYE
     AHHKVAISDT ALVAAATLSH RYITSRFLPD KAIDLIDEAA SRLRMEIDSR PVEIDELQRT
     VDRMKMEELA LAKEHDPASR DRLARLRLDL ADRQEQLNAL NARWEQEKSG LNRVGELKQR
     LDAMKSQVEQ AQRSGDFETA SRLLYAEIPA VEAELETAST TVDEAEDVAP MVKEEVGPDD
     IAEVVGAWTG IPAGRLLEGE TEKLLTMEQR IGERLIGQAE AVAAVSDAVR RARAGISDPD
     RPTGSFLFLG PTGVGKTELA KALADFLFDD EHAMVRIDMS EYSEKHSVAR LVGAPPGYVG
     YEEGGQLTEA VRRRPYSVVL LDEVEKAHPE IFDVLLQVLD DGRLTDGQGR TVDFRNTILI
     LTSNLGTSGF DLTVDEALDP VQARLDRRQR VDNAVRAAFK PEFLNRLDAQ VIFDPLGTTE
     LGRIVDIQVR KLAARLADRR LGLEVTPGAR DWLAIAGYEP AFGARPLRRL VQSSIGDPLA
     RRLLAGEIRD GDTVRVDVDI ENDALIIGSQ AS
//

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