HTPG_ECOK1
ID HTPG_ECOK1 Reviewed; 624 AA.
AC A1A8D9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=Ecok1_04350;
GN ORFNames=APECO1_1542;
OS Escherichia coli O1:K1 / APEC.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=405955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17293413; DOI=10.1128/jb.01726-06;
RA Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT shares strong similarities with human extraintestinal pathogenic E. coli
RT genomes.";
RL J. Bacteriol. 189:3228-3236(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; CP000468; ABI99928.1; -; Genomic_DNA.
DR RefSeq; WP_000678211.1; NC_008563.1.
DR AlphaFoldDB; A1A8D9; -.
DR SMR; A1A8D9; -.
DR EnsemblBacteria; ABI99928; ABI99928; APECO1_1542.
DR KEGG; ecv:APECO1_1542; -.
DR HOGENOM; CLU_006684_3_0_6; -.
DR OMA; MRRMKEM; -.
DR Proteomes; UP000008216; 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; Stress response.
FT CHAIN 1..624
FT /note="Chaperone protein HtpG"
FT /id="PRO_1000014914"
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; 71437 MW; 72CB4DD14230560E CRC64;
MKGQETRGFQ SEVKQLLHLM IHSLYSNKEI FLRELISNAS DAADKLRFRA LSNPDLYEGD
GELRVRVSFD KDKRTLTISD NGVGMTRDEV IDHLGTIAKS GTKSFLESLG SDQAKDSQLI
GQFGVGFYSA FIVADKVTVR TRAAGEKPEN GVFWESAGEG EYTVADITKE DRGTEITLHL
REGEDEFLDD WRVRSIISKY SDHIALPVEI EKREEKDGET VISWEKINKA QALWTRNKSE
ITDEEYKEFY KHIAHDFNEP LTWSHNRVEG KQEYTSLLYI PSQAPWDMWN RDHKHGLKLY
VQRVFIMDDA EQFMPNYLRF VRGLIDSSDL PLNVSREILQ DSTVTRNLRN ALTKRVLQML
EKLAKDDAEK YQTFWQQFGL VLKEGPAEDF ANQEAIAKLL RFASTHTDSS AQTVSLEDYV
SRMKEGQEKI YYITADSYAA AKSSPHLELL RKKGIEVLLL SDRIDEWMMN YLTEFDGKPF
QSVSKVDESL EKLADEVDES AKEAEKALTP FIDRVKALLG ERVKDVRLTH RLTDTPAIVS
TDADEMSTQM AKLFAAAGQK VPEVKYIFEL NPDHVLVKRA ADTEDEAKFS EWVELLLDQA
LLAERGTLED PNLFIRRMNQ LLVS