HTPG_CLOBH
ID HTPG_CLOBH Reviewed; 626 AA.
AC A5I3B0; A7G4S0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Chaperone protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE AltName: Full=Heat shock protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE AltName: Full=High temperature protein G {ECO:0000255|HAMAP-Rule:MF_00505};
GN Name=htpG {ECO:0000255|HAMAP-Rule:MF_00505};
GN OrderedLocusNames=CBO1985, CLC_1931;
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
CC -!- FUNCTION: Molecular chaperone. Has ATPase activity. {ECO:0000255|HAMAP-
CC Rule:MF_00505}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00505}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00505}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000255|HAMAP-Rule:MF_00505}.
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DR EMBL; CP000727; ABS38135.1; -; Genomic_DNA.
DR EMBL; AM412317; CAL83528.1; -; Genomic_DNA.
DR RefSeq; WP_011986521.1; NC_009698.1.
DR RefSeq; YP_001254488.1; NC_009495.1.
DR RefSeq; YP_001387785.1; NC_009698.1.
DR AlphaFoldDB; A5I3B0; -.
DR SMR; A5I3B0; -.
DR GeneID; 5186240; -.
DR KEGG; cbh:CLC_1931; -.
DR KEGG; cbo:CBO1985; -.
DR PATRIC; fig|413999.7.peg.1959; -.
DR HOGENOM; CLU_006684_3_0_9; -.
DR OMA; MRRMKEM; -.
DR PRO; PR:A5I3B0; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF00183; HSP90; 2.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW Stress response.
FT CHAIN 1..626
FT /note="Chaperone protein HtpG"
FT /id="PRO_1000014912"
FT REGION 1..341
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 342..552
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 490..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..626
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 626 AA; 72853 MW; 89479037EAE3A97E CRC64;
METKQFKAES KRLLDLMINS IYTHKEIFLR ELISNSSDAI DKIYYKTLTD DSLKFERDNY
YIRVVSDKEN RILKIADTGI GMTKEELENN LGVIAKSGSL QFKKENEVKE GYDIIGQFGV
GFYSAFLVSD DVTVISKAFG SNEAYKWNSK GAEGYTIEPC EKETYGTEII LKIKDNTEEE
NYDEFLEEYT LKSIIKKYSD FIRYPIKMDL TKTKPKEDNK EEFEEYKEEE TINSMVPIWR
KNKNELKAED YENFYAEKHY GFDKPIKYIH TSVDGVVSYN AILFIPETTP YDFYTKEYEK
GLELYSSGVL IMNKCGDLLP DYFGFVKGIV DSEDLSLNIS REILQHDRQL KLIAKNIKTK
IKNELESLLK KERDKYEKFY ESFGRQLKYG VYSDFGSNKD ILQDLLMFYS SKEKKMVTLA
EYVSRMPEDQ KYIYYAVGES NERIEKLPQI EGVLDKGYEV LYFTDDIDEF AIKMLMSYKE
KEFKSVSSGD LGIEGEEKEN TSNSDDKENK ELFESMKDML SGKVKDVRAS KRLKNHPVCL
ANEGELSIEM EKVLNAMPNN QNIKADKVLE ININHDVFKS LKEAYEGDKE KLKLYTDLLY
NQALLIEGLA INDPVEFTNN ICKIMK
