ID A0A1S6HMT6_9GAMM Unreviewed; 638 AA.
AC A0A1S6HMT6;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=Sps_01668 {ECO:0000313|EMBL:AQS36833.1};
OS Shewanella psychrophila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=225848 {ECO:0000313|EMBL:AQS36833.1, ECO:0000313|Proteomes:UP000189545};
RN [1] {ECO:0000313|EMBL:AQS36833.1, ECO:0000313|Proteomes:UP000189545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP2 {ECO:0000313|EMBL:AQS36833.1,
RC ECO:0000313|Proteomes:UP000189545};
RA Xu G., Jian H.;
RT "Complete genome sequence of Shewanella psychrophila WP2, a deep sea
RT bacterium isolated from west Pacific sediment.";
RL Submitted (MAR-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; CP014782; AQS36833.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S6HMT6; -.
DR STRING; 225848.Sps_01668; -.
DR KEGG; spsw:Sps_01668; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000189545; 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00505}; Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 27..184
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..346
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 564..638
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 638 AA; 71501 MW; CDB24A0E9AD011F6 CRC64;
MSQQETHGFQ TEVKQLLNLM IHSLYSNKEI FLRELVSNAA DAADKLRYEA LTNDALYEGD
GELSVRISAD KDKGTITISD NGIGMTRDGV IEHLGTIAKS GTAEFFNNLS GDDTKDSQLI
GQFGVGFYSS FIVADKVTVR TRAAGHSADE GVLWESAGEG DFTVDNITKE TRGTEIVLHL
RKEEQEFADD YRLRSIITKY SDHISVPVEM FEEGTPAIEA SDDQEAVAAV EGSWKPMNKA
TALWTRNKSD ISKEEYEEFY KHISHDFTDP LLWSHNRVEG KQEYTSLLYI PAKAPWDMWN
RDRKHGLKLF VQRVFVMDDA EQFMPSYLRF VQGLIDSNDL PLNVSREILQ DNKVTTALRT
AVTKRVLSML EKLAKNDAEK YQTFWAEFGQ VLKEGPAEDM ANKERIAGLL RFASTHTEGA
APTVSLADYI GRMQEGQNKI YYIVADSHEA AANSPHLELL RKKGIEVLLM SERIDEWLIN
HLTDFDGKQL HSVTRGDLEL GDLEDAGEKE AQEKMETESE GLVKRVKDSL GDKVSAVKVT
TRLTDTPACV VAGEGEMSTQ MIKLMEAAGQ AVPESKPTFE INPEHPLVAR LDDEQDEAVF
TQWTELLLQQ AQLSEKGSLA DPSAFIKLMN QMLLAKLK
//
