HTPG_BACSU
ID HTPG_BACSU Reviewed; 626 AA.
AC P46208;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 140.
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}; Synonyms=yxbB;
GN OrderedLocusNames=BSU39820; ORFNames=SS92A;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BGSC1A1;
RX PubMed=7584049; DOI=10.1093/dnares/2.2.61;
RA Yoshida K., Seki S., Fujimura M., Miwa Y., Fujita Y.;
RT "Cloning and sequencing of a 36-kb region of the Bacillus subtilis genome
RT between the gnt and iol operons.";
RL DNA Res. 2:61-69(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
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; AB005554; BAA21603.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16018.1; -; Genomic_DNA.
DR PIR; H69642; H69642.
DR RefSeq; NP_391861.1; NC_000964.3.
DR RefSeq; WP_003243561.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P46208; -.
DR SMR; P46208; -.
DR IntAct; P46208; 1.
DR STRING; 224308.BSU39820; -.
DR jPOST; P46208; -.
DR PaxDb; P46208; -.
DR PRIDE; P46208; -.
DR EnsemblBacteria; CAB16018; CAB16018; BSU_39820.
DR GeneID; 937631; -.
DR KEGG; bsu:BSU39820; -.
DR PATRIC; fig|224308.179.peg.4308; -.
DR eggNOG; COG0326; Bacteria.
DR InParanoid; P46208; -.
DR OMA; MRRMKEM; -.
DR PhylomeDB; P46208; -.
DR BioCyc; BSUB:BSU39820-MON; -.
DR Proteomes; UP000001570; 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; 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; 2.
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_0000062968"
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; 72258 MW; 75A06B9EE5FE9F68 CRC64;
MAKKEFKAES KRLLDMMINS IYTQKEIFLR ELISNSSDAI DKIYYKALTD DALTFDKDSY
YIKVAADKDA RTLTISDTGI GMTKDELEQH LGTIAKSGSL AFKKENELKD GHDIIGQFGV
GFYAAFMVAD VVTVISKALG SEEAYKWESA GADGYTIEPC EKDSVGTDII LKIKENTEDD
SYDEFLEEYR LKAIIKKYSD FIRYPIKMDT TINKPKEGSE NEFEEVQEEQ TVNSMVPIWR
KNKSELTDED YEKFYAEKHY GFDKPLTHVH ISVDGAVRYN AILFVPENMP FDYYSKEYEK
GLELYSNGVL IMNKCADLLP DHFSFVKGMV DSEDLSLNIS REMLQHDRQL KLIAKNISKK
IKSELQSLLK KDREKYETFY KSFGRQLKFG VYNDFGANKD QLKDLLLFYS SKEKKLVSLD
EYVSRMPEEQ KFIYYATGDS YDRIEKLPQT EMVADKGYEI LYFTEDIDEF AIKMLASYQE
KEFKSVSSGD LGIDTDEDQK QSEEEESKYK DLFEEMKNIL SDKVKNVRIS KRLKSHPVCL
AADGEVTIEM EKILNAMPDS QNVKAEKVLE INPNHEVFQT LQDAFEQDKE KLSLYTNLLY
NQALLIEGLP IQDPVEFTNN ICKVMV
