ID A0A1Y2SQL1_9GAMM Unreviewed; 631 AA.
AC A0A1Y2SQL1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=Xbed_00520 {ECO:0000313|EMBL:OTA21293.1};
OS Xenorhabdus beddingii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=40578 {ECO:0000313|EMBL:OTA21293.1, ECO:0000313|Proteomes:UP000194204};
RN [1] {ECO:0000313|EMBL:OTA21293.1, ECO:0000313|Proteomes:UP000194204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4764 {ECO:0000313|EMBL:OTA21293.1,
RC ECO:0000313|Proteomes:UP000194204};
RA Tobias N.J., Wolff H., Djahanschiri B., Ebersberger I., Bode H.B.;
RT "Deconstructing symbiosis and pathogenesis requirements using a combined
RT genomic-metabolomic approach.";
RL Submitted (JAN-2017) 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: 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:OTA21293.1}.
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; MUBK01000003; OTA21293.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2SQL1; -.
DR STRING; 40578.Xbed_00520; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000194204; 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|HAMAP-Rule:MF_00505,
KW ECO:0000313|EMBL:OTA21293.1}.
FT DOMAIN 29..186
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..340
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 341..556
FT /note="B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 557..631
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 631 AA; 71828 MW; 3673CD5BFED8670A CRC64;
MNMKGQETRG FQSEVKQLLQ LMIHSLYSNK EIFLRELISN ASDAADKLRF RALSTPELYE
NDGELRVRLA VDKEQKTITI SDNGIGMSRD EVIDNLGTIA KSGTKAFLES IGSDQAKDSQ
LIGQFGVGFY SAFIVADKVT VRTRAAGSAA DQGVFWESTG EGDYTVADIE KTERGTEITL
HLRDSESEFL NDWRLRSIIG KYSDHIALPV EIETQTQDEE NDTVTVSWEK INKAQALWTR
GKAEISDEEY QEFYKHISHD FTDSLIWSHN RVEGKQEYTS LLYIPSQAPW DMWNREHKHG
LKLYVQRVFI MDEADQFMPN YLRFVRGLID SNDLPLNVSR EILQDSTVTR NLRSALTKRV
LQMLDKLAKD DAEKYQTFWQ QFGLVLKEGP AEDGTNKEAI AKLLRFATTH HDGSTQNVSL
EEYVSRMAEG QEKIYYITAD SYAAAKNSPH LELFRKKGIE VLLLSDRIDE WMMSYLTEFD
GKSLQSVSKS DESLDKLADE NKAEQEDADK KLEPFIERVK TLLGERVKEV KLTHRLTDTP
AIVTTDANGM STQMAKLFAA AGQSAPEVSY NFELNPEHNL VKKAADIDDE AQFADWIELL
LEQALFAERG TLDDPNQFIR RMNQLLLAET A
//
