ID D0LYJ5_HALO1 Unreviewed; 657 AA.
AC D0LYJ5;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
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 OrderedLocusNames=Hoch_5377 {ECO:0000313|EMBL:ACY17861.1};
OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY17861.1, ECO:0000313|Proteomes:UP000001880};
RN [1] {ECO:0000313|EMBL:ACY17861.1, ECO:0000313|Proteomes:UP000001880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2
RC {ECO:0000313|Proteomes:UP000001880};
RX PubMed=21304682; DOI=10.4056/sigs.69.1277;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL Stand. Genomic Sci. 2:96-106(2010).
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 ---------------------------------------------------------------------------
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; CP001804; ACY17861.1; -; Genomic_DNA.
DR RefSeq; WP_012830453.1; NC_013440.1.
DR AlphaFoldDB; D0LYJ5; -.
DR STRING; 502025.Hoch_5377; -.
DR KEGG; hoh:Hoch_5377; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_7; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000001880; 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: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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00505}; Reference proteome {ECO:0000313|Proteomes:UP000001880};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505,
KW ECO:0000313|EMBL:ACY17861.1}.
FT DOMAIN 36..193
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..358
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 576..657
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT COILED 510..537
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 657 AA; 73928 MW; 8DE18A7F74967E3B CRC64;
MATTDASAPQ EGQAHYEFRA ETQQLLRLMI HSLYSNKEIF LRELISNASD ALDKLRFAAL
TDQSLVPEEE LHIRIEIDAE ARSLTVHDNG IGMSREDAVQ NLGTIAKSGT QEFMALLEQA
KDAKERPDLI GQFGVGFYAS FLVADRVVVL TRKAGEVEAT RWESDGVGGS YTVEAAERPQ
AGTSVTLMLK PADDEDGIQD YTKPWVVESI VRKYSDFVSY PIKMKQEAPP LAKPDEEAPP
AEPEDKVLNS MKAIWTRSPS DVQDEEYKEF YKHISHDWND PLTHLTTSLE GTLEAKALLY
IPSRAPFDLF RADAERRGVQ LYVRRVFIMD DCKELLPNYL RFVRGVVDSE DLPLNVSREI
LQQNRQIRAI RKHLVKKILD ALANMKKGEG DDYLSFWKQF GAVLKEGLLL SQERNERIYE
LLLAESSNGE AGALVSLGEY SERMKEGQEA IYYLTAPSVE QARKSPHLEA FQAKGVEVLF
FTDAVDEIWL QERAEYEGKK FQSVVQGDIQ LGTEEEKKEA EEEKQRQQNE LGDLLLAVRA
ALQEEVKEVR LSSRLTSSPA CLVTGDGDLS PQLERIMRAT GQEVPKVKRV LEVNPTHPVV
KRMQEMHEAS KAHPDLPNFS RLLYGQAILS EGGELEEPAE FAKLIAEVMV KVSVSAS
//
