HTPG_BACLD
ID HTPG_BACLD Reviewed; 626 AA.
AC Q65CZ5; Q62NH1;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=BLi04256, BL00247;
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
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; AE017333; AAU43069.1; -; Genomic_DNA.
DR EMBL; CP000002; AAU25690.1; -; Genomic_DNA.
DR RefSeq; WP_003177835.1; NC_006322.1.
DR AlphaFoldDB; Q65CZ5; -.
DR SMR; Q65CZ5; -.
DR STRING; 279010.BL00247; -.
DR PRIDE; Q65CZ5; -.
DR EnsemblBacteria; AAU25690; AAU25690; BL00247.
DR GeneID; 66213815; -.
DR KEGG; bld:BLi04256; -.
DR KEGG; bli:BL00247; -.
DR PATRIC; fig|279010.13.peg.4340; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_9; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 246194at2; -.
DR BioCyc; BLIC279010:BLI_RS20930-MON; -.
DR Proteomes; UP000000606; Chromosome.
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:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
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; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
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_0000224197"
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 553..626
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 626 AA; 72031 MW; 37E1395DA28D1F6B CRC64;
MAKREFKAES KRLLDIMINS IYSQKEVFLR ELISNASDAI DKIYYKALTD DSLTFNKDDY
YIKISADKEN RTLTIADTGI GMTKEELEEH LGTIAKSGSL AFKQENELKD GHDIIGQFGV
GFYAAFMVAD TVTVITKAHG SDEAHQWESA GADGYTIEPA AKESAGTDVI LKLKENTDDE
NYDEYLDVHR LKAIIKTYSD FIRYPIKMDV AVNKPKEGAE NEFEEVQEEQ TVNSMVPIWR
KNKSELKDED YEAFYKEKHY GFDKPLAHIH TSVDGAVRYH AILFIPENIP FNYYTKEFEK
GLELYSNGVL IMEKCPDLLP DHFSFVKGMV DSEDLSLNIS REMLQHDRQL KLIAKNISKK
IKNELKSLLK NDREKYESFY QSFGRQLKFG VYNDFGAHKD LLKDLLLFYS SKEKKLVTLE
EYVSRMPEDQ KYIYYASGDS YDRIEKLPQT ELVSEKGYEI LYFTEDIDEF AIKMLANYQE
KEFKSVSSGD LGIENDDEQN QSDGDDSQYK DLFEEMKKTL DGKVKSVRAS KRLKTHSVCL
AADGEVTIEM EKILNAMPDN QHVKADKVLE INTNHEVFKT LQNAFDNDKD KFKLYTGLLY
NQALLIEGLP IEDPVEFTND ICKVMA
