GenomeNet

Database: UniProt
Entry: Q9I3C5
LinkDB: Q9I3C5
Original site: Q9I3C5 
ID   HTPG_PSEAE              Reviewed;         634 AA.
AC   Q9I3C5;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 126.
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=PA1596;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE004091; AAG04985.1; -; Genomic_DNA.
DR   PIR; A83447; A83447.
DR   RefSeq; NP_250287.1; NC_002516.2.
DR   RefSeq; WP_003087446.1; NZ_QZGE01000003.1.
DR   AlphaFoldDB; Q9I3C5; -.
DR   SMR; Q9I3C5; -.
DR   IntAct; Q9I3C5; 1.
DR   MINT; Q9I3C5; -.
DR   STRING; 208964.PA1596; -.
DR   PaxDb; 208964-PA1596; -.
DR   GeneID; 881933; -.
DR   KEGG; pae:PA1596; -.
DR   PATRIC; fig|208964.12.peg.1656; -.
DR   PseudoCAP; PA1596; -.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   InParanoid; Q9I3C5; -.
DR   OrthoDB; 9802640at2; -.
DR   PhylomeDB; Q9I3C5; -.
DR   BioCyc; PAER208964:G1FZ6-1626-MONOMER; -.
DR   Proteomes; UP000002438; 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:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0006974; P:DNA damage response; 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   CDD; cd16927; HATPase_Hsp90-like; 1.
DR   Gene3D; 3.30.230.80; -; 1.
DR   Gene3D; 3.40.50.11260; -; 1.
DR   Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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_Su5_D2-typ_SF.
DR   PANTHER; PTHR11528:SF97; ENDOPLASMIN; 1.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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..634
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000063003"
FT   REGION          1..342
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          343..559
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          560..634
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   634 AA;  71668 MW;  ACD96C46206ECB55 CRC64;
     MSVETQKETL GFQTEVKQLL HLMIHSLYSN KEIFLRELIS NASDAADKLR FEALANPELL
     EGGAELKIRV SFDKEANTVT LEDNGIGMSR EDVVTHLGTI AKSGTADFLK NLSGDQKKDS
     HLIGQFGVGF YSAFIVADKV DVYSRRAGQP ASEGVHWSSK GEGEFDVATI DKPERGTRIV
     LHLKKGEEEF ADGWRLRNVI KKYSDHIALP IELPKEFHGE EADKPAEPEW ETVNRASALW
     TRPRAEVKDE EYQEFYKHVA HDFENPLSWS HNKVEGKLEY TSLLYVPGRA PFDLYHREAP
     RGLKLYVQRV FIMDQADEFL PLYLRFIKGV VDSNDLSLNV SREILQKDPV IDSMKSALTK
     RVLDMLEKLA KNEPEQYKTF WKNFGQVLKE GPAEDFGNKE KIAGLLRFAS TGDDSGEQSV
     ALADYIGRMK EGQDKIYYLT GESYSQVKNS PHLEVFRKKG IEVLLLTDRI DEWLMSYLPE
     FDGKQFVDVA RGDLDLGSLD SEEDKKAQEE VAKSKEGLIE RLKKVLDEQV SEVRVSHRLT
     DSPAILAIGE QDLGLQMRQI LEASGQKVPD SKPIFEINPQ HPLIEKLDAE PDEDRFGELS
     HILFDQAALA AGDSLKDPGA YVRRLNKLLV ELSA
//
DBGET integrated database retrieval system