HTPG_PSEU2
ID HTPG_PSEU2 Reviewed; 635 AA.
AC Q4ZUW2;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 25-MAY-2022, entry version 105.
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=Psyr_2017;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY37060.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000075; AAY37060.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_003406139.1; NC_007005.1.
DR RefSeq; YP_235098.1; NC_007005.1.
DR AlphaFoldDB; Q4ZUW2; -.
DR SMR; Q4ZUW2; -.
DR STRING; 205918.Psyr_2017; -.
DR EnsemblBacteria; AAY37060; AAY37060; Psyr_2017.
DR KEGG; psb:Psyr_2017; -.
DR PATRIC; fig|205918.7.peg.2060; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_6; -.
DR Proteomes; UP000000426; 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..635
FT /note="Chaperone protein HtpG"
FT /id="PRO_0000224224"
FT REGION 1..343
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 344..560
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 561..635
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 635 AA; 71332 MW; C9292450E9094E39 CRC64;
MSVETQKETL GFQTEVKQLL HLMIHSLYSN KEIFLRELIS NASDAVDKLR FEALSKPELL
EGGAELKIRV SFDKDAKTVT LEDNGIGMSR EDVITHLGTI AKSGTADFMK NLSGDQKKDS
HLIGQFGVGF YSAFIVADQV EVFSRRAGTP ASEGVHWSSK GEGEFEVATV DKADRGTRIV
LHLKNGEEEF ADGYRLRNII KKYSDHIALP IELPKEQAPA AEGEEPAALE WETVNRASAL
WTRPRTEVKD EEYQEFYKHV AHDYENPLSW SHNKVEGKLE YTSLLYVPAR APFDLYQREA
PRGLKLYVQR VFVMDQAESF LPLYMRFVKG VVDSNDLSLN VSREILQKDP IIDSMKSALT
KRVLDMLEKL AKNEPEKYKG FWKNFGQVLK EGPAEDFANK EKIAGLLRFA STSDDSGEQS
VSLAEYLARA KEGQDKIYYL TGESYAQVKN SPHLEVFRKK GIEVLLLTDR IDEWLMSYLS
DFDGKGFVDV ARGDLDLGNL DSEEDKKAQE EIAKDKEGLI ERLKAALGES VSEVRVSHRL
TDSPAILAIG EQDMGLQMRQ ILEASGQKVP DSKPIFEFNP AHPLIGKLDA EQSEDRFGDL
SHILFDQAAL AAGDSLKDPA AYVRRLNKLL VELSV