ID B9B4U3_9BURK Unreviewed; 632 AA.
AC B9B4U3;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=Chaperone protein HtpG {ECO:0000256|HAMAP-Rule:MF_00505};
DE AltName: Full=Heat shock protein HtpG {ECO:0000256|HAMAP-Rule:MF_00505};
DE AltName: Full=High temperature protein G {ECO:0000256|HAMAP-Rule:MF_00505};
GN Name=htpG {ECO:0000256|HAMAP-Rule:MF_00505,
GN ECO:0000313|EMBL:EEE01458.1};
GN ORFNames=BURMUCGD1_0858 {ECO:0000313|EMBL:EEE01458.1};
OS Burkholderia multivorans CGD1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=513051 {ECO:0000313|EMBL:EEE01458.1, ECO:0000313|Proteomes:UP000005493};
RN [1] {ECO:0000313|EMBL:EEE01458.1, ECO:0000313|Proteomes:UP000005493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGD1 {ECO:0000313|EMBL:EEE01458.1,
RC ECO:0000313|Proteomes:UP000005493};
RX PubMed=23105085; DOI=10.1128/JB.01306-12;
RA Varga J.J., Losada L., Zelazny A.M., Brinkac L., Harkins D., Radune D.,
RA Hostetler J., Sampaio E.P., Ronning C.M., Nierman W.C., Greenberg D.E.,
RA Holland S.M., Goldberg J.B.;
RT "Draft Genome Sequence Determination for Cystic Fibrosis and Chronic
RT Granulomatous Disease Burkholderia multivorans Isolates.";
RL J. Bacteriol. 194:6356-6357(2012).
CC -!- FUNCTION: Molecular chaperone. Has ATPase activity. {ECO:0000256|HAMAP-
CC Rule:MF_00505}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00505}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239, ECO:0000256|HAMAP-Rule:MF_00505}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00505}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEE01458.1}.
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DR EMBL; ACFB01000003; EEE01458.1; -; Genomic_DNA.
DR RefSeq; WP_006398689.1; NZ_ACFB01000003.1.
DR AlphaFoldDB; B9B4U3; -.
DR Proteomes; UP000005493; Unassembled WGS sequence.
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:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00505};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00505};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00505};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00505}.
FT DOMAIN 26..183
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..339
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 560..632
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 632 AA; 71276 MW; 3D76F19164E077E2 CRC64;
MAHETMSFQA EVKQLLHLMI HSLYSNKEIF LRELVSNASD AADKLRFEAL ADNALYEDDP
NLRIRIGYDK AARTITIDDN GIGMSRDEAI ANLGTIARSG TKEFFSKLSG DQQKDAALIG
QFGVGFYSGF IVADKITVET RRAGLSASEG VRWESAGEGD FTIDAIERAQ RGTTITLHLR
EGEDELLSSY RLKSIIQKYS DHIALPILMK KEEWDQEKGE MVVKDDDETV NQASALWTRP
KSEITDEQYK QFYQHIAHDH QDPLTWTHNR VEGRSEYTQL LYVPSQAPFD LWNRDYRGGL
KLYVKRVFIM DDAEQLLPQY LRFVKGVVDS ADLPLNVSRE ILQESRDVKA IREGVTKRAL
SMLEELANAE DDAGKEKYKT FWRAFGQVLK EGVGEDHANR ERIAKLLRFA STHGDTDAQD
VSLADYVARM KPEQTKIYYV TADTWQAAKN SPHLEVFRKK GVEVLLLTDR VDEWMLSFLH
EFDGKPLASV ARGDLDLGAL NDEEKKAQEE AGEAIKPVVE KMKEALGDKV KDVRVTFRLT
DSPSCLVADD NDMSGYLQRM LKAAGQKAPS FQPILEINPE HALVKQLKAD SADFGDWCHL
LFDQALLAEG GMLDDPASFV KRTNALLLSR AA
//
