ID A0A0M5IY74_SPHS1 Unreviewed; 626 AA.
AC A0A0M5IY74;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=LH20_22765 {ECO:0000313|EMBL:ALC14794.1};
OS Sphingopyxis sp. (strain 113P3).
OG Plasmid unnamed {ECO:0000313|EMBL:ALC14794.1}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=292913 {ECO:0000313|EMBL:ALC14794.1, ECO:0000313|Proteomes:UP000061305};
RN [1] {ECO:0000313|EMBL:ALC14794.1, ECO:0000313|Proteomes:UP000061305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=113P3 {ECO:0000313|EMBL:ALC14794.1,
RC ECO:0000313|Proteomes:UP000061305};
RC PLASMID=Plasmid {ECO:0000313|Proteomes:UP000061305};
RX PubMed=26472829;
RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA Tsuda M., Fujita N., Kawai F.;
RT "Complete Genome Sequence of Polyvinyl Alcohol-Degrading Strain
RT Sphingopyxis sp. 113P3 (NBRC 111507).";
RL Genome Announc. 3:e01169-15(2015).
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; CP009453; ALC14794.1; -; Genomic_DNA.
DR RefSeq; WP_053556580.1; NZ_CP009453.1.
DR AlphaFoldDB; A0A0M5IY74; -.
DR KEGG; sphp:LH20_22765; -.
DR PATRIC; fig|292913.6.peg.4673; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000061305; Plasmid.
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}; Plasmid {ECO:0000313|EMBL:ALC14794.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000061305};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00505}.
FT DOMAIN 32..190
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..335
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 551..626
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 626 AA; 68875 MW; 38D15689845CC23A CRC64;
MTTTLDAAPE TRSFETDVAK LLHLMVHSVY SDKDVFLREL ISNAADACEK LRYEMLSHPE
LGSGELPRIT VTLDLDQRRL IVEDNGIGMN EAEMIEALGT IARSGTKAFM ERVASAKDAE
GAQLIGQFGV GFYSAFMVAD KVDVFSRRAG GDTAAHWSSD GLGTYSVEIA ELADAPTHGT
RVVLELKEDA AQYAQRFNSE GIIKAQSGHV PVPIFLLEKP DAEPVQIGDG AALWTKPKSE
ISEEDYTDFY RSVAGQFDKP ALTLHYRAEG LHEYSVLAFI PEMKPFDLFD PERHGRMKLY
VKRVFITDEA EILPRYLRFV RGLVDSSDIP LNVSREMIQE SPVLAAIQKG VANRLLSELE
KLSTNDADAY QQFWMNFGAV LKEGLYEDYG RRETLLGLAR FKTTTSGTEW RSLKDYVAAI
KENQTAIYYA TGPDLDRLAS SPQLEGFRAR GIEVLLLTDQ VDSFWVTAGL DFEGKPFKSV
TQGSADLGLI PLTEGDAPAA STSDEVSGFI EFVKEVLKDE VSDVRASERL TESAACLVAP
EHGMDRQLEK LLAASGRGGT AARPVLEINP RHDLVQKLAG LAADADLRED SARLLLDEAR
IADGELPADP RGFAARLGRI WTKALA
//
