ID A0A157ZUN3_9BURK Unreviewed; 634 AA.
AC A0A157ZUN3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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 ORFNames=AWB78_00959 {ECO:0000313|EMBL:SAK49200.1};
OS Caballeronia calidae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=1777139 {ECO:0000313|EMBL:SAK49200.1, ECO:0000313|Proteomes:UP000071859};
RN [1] {ECO:0000313|EMBL:SAK49200.1, ECO:0000313|Proteomes:UP000071859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29321 {ECO:0000313|EMBL:SAK49200.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FCOX02000003; SAK49200.1; -; Genomic_DNA.
DR RefSeq; WP_062602747.1; NZ_FCOX02000003.1.
DR AlphaFoldDB; A0A157ZUN3; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000071859; 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 564..634
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 634 AA; 71649 MW; 042A064308A7C91F CRC64;
MAQETMSFQA EVKQLLHLMI HSLYSNKEIF LRELISNASD AADKLRFEAI ENSALYESDP
DLRIRVSFDK AARTVTIDDN GIGMSRDEAI SHLGTIARSG TKEFFSKLSG DQQKDAALIG
QFGVGFYSGF IVADKITVET RRAGLPSNQG VRWTSAGEGD FEVEDIERAQ RGTTITLHLR
ADEDELLSTH RLKSIIQKYS DHVALPILMK KEEWDAEKSE MVTKDEDETV NQASALWTRP
KNDISDDQYK QFYQHISHDH DDPLAWTHNR VEGRSEYTQL LYVPKHAPFD LWNREHRGGL
KLYVKRVFIM DDAEQLLPAY LRFVKGVVDS ADLPLNVSRE LLQESRDVKA IREGVTKRVL
SMLEEIATSS AEATEDADKQ KYATFWNEFG QVLKEGIGED FGNRERIAKL VRFASTNNDS
DEQNVSLADY VARMKPEQTK IYYVTADSWQ AAKHSPHLEV FRKKGVEVLL LTDRVDEWML
SFLNEFDGKP LQSVARGDLD LGALDDEEKQ QQEKVGEEMK PLVEKMKEAL EGKAKDVRLT
FRLTDSPSCL VADEGDMSGY LQRMLKAAGQ KAPQAEPILE VNPEHPLVKA LNADSANFAD
WCHLLFDQAL LAEGGALDDP ASFVKRTNAL LLAR
//
