ID   HTPG_PSEFS              Reviewed;         636 AA.
AC   C3K6N7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 86.
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}; OrderedLocusNames=PFLU_1830;
OS   Pseudomonas fluorescens (strain SBW25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=216595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SBW25;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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; AM181176; CAY48077.1; -; Genomic_DNA.
DR   AlphaFoldDB; C3K6N7; -.
DR   SMR; C3K6N7; -.
DR   STRING; 294.SRM1_01622; -.
DR   PRIDE; C3K6N7; -.
DR   EnsemblBacteria; CAY48077; CAY48077; PFLU_1830.
DR   KEGG; pfs:PFLU_1830; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000002332; 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; PF02518; HATPase_c; 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..636
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000206569"
FT   REGION          1..344
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          345..561
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          562..636
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   636 AA;  71633 MW;  984122A5EFF0CF11 CRC64;
     MTMSVETQKE TLGFQTEVKQ LLHLMIHSLY SNKEIFLREL ISNASDAVDK LRFEALSKPE
     LLEGGAELKI RVSFDKDAKT VTLEDNGIGM SREDAITHLG TIAKSGTADF MKNLSGDQKK
     DSHLIGQFGV GFYSAFIVAD KVEVFSRRAG LDASEGVHWS SKGEGEFEIA TVDKADRGTR
     IVLHLKDGED EFADGWRLRN IVKKYSDHIA LPIELPKEQA AAEGEETPAQ EWEVVNRASA
     LWTRPRTEIK DEEYQEFYKH IGHDYENPLS WSHNKVEGKL EYSSLLYVPA RAPFDLYQRE
     APKGLKLYVQ RVFVMDQAES FLPLYLRFIK GVVDSNDLSL NVSREILQKD PIIDSMKSAL
     TKRVLDMLEK LAKNEPEQYK GFWKNFGQVM KEGPAEDFAN KEKIAGLLRF ASTQGDDGEQ
     VVSLAEYLAR AKEGQDKIYY LTGETYAQVK NSPHLEVFRK KGIEVLLLTD RIDEWLMSYL
     NEFDGKSFVD VARGDLDLGN LDSEEEKKEA EEVAKSKEGL VERIKASLGD AVSEVRVSHR
     LTDSPAILAI GEQDLGMQMR QILEASGQKV PDSKPIFEFN PAHPLIEKLD GEQSEERFGD
     LSHILFDQAA LAAGDSLKDP AAYVRRLNKL LVELSV