HTPG_KLEP7
ID HTPG_KLEP7 Reviewed; 624 AA.
AC A6T5N6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=KPN78578_04460; ORFNames=KPN_00455;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000647; ABR75907.1; -; Genomic_DNA.
DR RefSeq; WP_004177228.1; NC_009648.1.
DR AlphaFoldDB; A6T5N6; -.
DR SMR; A6T5N6; -.
DR STRING; 272620.KPN_00455; -.
DR jPOST; A6T5N6; -.
DR EnsemblBacteria; ABR75907; ABR75907; KPN_00455.
DR GeneID; 61331606; -.
DR GeneID; 64296691; -.
DR KEGG; kpn:KPN_00455; -.
DR HOGENOM; CLU_006684_3_0_6; -.
DR OMA; MRRMKEM; -.
DR Proteomes; UP000000265; 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..624
FT /note="Chaperone protein HtpG"
FT /id="PRO_1000014925"
FT REGION 1..336
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 337..552
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 553..624
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 624 AA; 71107 MW; 755F2FD5C5A19346 CRC64;
MKGQETRGFQ SEVKQLLHLM IHSLYSNKEI FLRELISNAS DAADKLRFRA LSQPDLYEGD
GELRVRVSFD KDNRTLTIAD NGIGMNREEV IDHLGTIAKS GTKAFLESMG SDQAKDSQLI
GQFGVGFYSA FIVADKVTVR TRAAGDKPEN GVFWESAGEG EYTVADITKA DRGTEITLHL
REGEDDFLND WRVRSIISKY SDHIALPVEI EKREEKDGET VISWEKINKA QALWTRSKSE
VNDDEYKEFY KHIAHDYSDP LTWSHNRVEG KQEYTSLLYI PSQAPWDMWN RDHKHGLKLY
VQRVFIMDDA EQFMPNYLRF VRGLIDSNDL PLNVSREILQ DSSVTRNLRT ALTKRALQML
DKLAKDDAEK YQTFWKQFGL VLKEGPAEDP SNQEAIAKLL RFATTHTDSS AQTVSLEEYV
SRMKEGQEKI YYITADSYAA AKSSPHLELL RKKGIEVLLL SDRIDEWMMS YLTEFDGKAF
QSVAKADESL DKLADEVDES TKEAEKALEP FVERVKNLLG DRVKEVRLTH RLTDTPAIVT
TDADEMSTQM AKLFAAAGQA APEVKYIFEL NPAHQLVKRA ADTQDDAQFG EWVELLLDQA
LLAERGTLED PNQFIRRMNQ LLAS