ID A0A2S0P7K9_9NEIS Unreviewed; 632 AA.
AC A0A2S0P7K9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=DAI18_04095 {ECO:0000313|EMBL:AVY93315.1};
OS Microvirgula aerodenitrificans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Aquaspirillaceae; Microvirgula.
OX NCBI_TaxID=57480 {ECO:0000313|EMBL:AVY93315.1, ECO:0000313|Proteomes:UP000244173};
RN [1] {ECO:0000313|EMBL:AVY93315.1, ECO:0000313|Proteomes:UP000244173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BE2.4 {ECO:0000313|EMBL:AVY93315.1,
RC ECO:0000313|Proteomes:UP000244173};
RA Anderson E., Jang J., Ishii S.;
RT "Denitrifier Microvirgula.";
RL Submitted (APR-2018) 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; CP028519; AVY93315.1; -; Genomic_DNA.
DR RefSeq; WP_028498034.1; NZ_CP028519.1.
DR AlphaFoldDB; A0A2S0P7K9; -.
DR STRING; 1122240.GCA_000620105_00560; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000244173; 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}; Reference proteome {ECO:0000313|Proteomes:UP000244173};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00505}.
FT DOMAIN 27..184
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 558..632
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 632 AA; 70660 MW; 42E6EB032E4A2DC7 CRC64;
MSEKQTLGFQ AEVKQLLQLM IHSLYSNKEI FLRELVSNAS DAADKLRFEA IANPALYEDD
AELKIRITFD ADARTLTIAD NGIGMSRDEV IEHIGTIAKS GTRAFFDSLT GDARKDANLI
GQFGVGFYSA FIVADRVTLT TRRAGLPADA GVRWESAGEG EYSIEAVDKA GRGTEIVLHL
REDEGELLND WRLRSILRKY SDHIAIPIEM LSTPEAADGD EPAPAAVFEP VNQASALWAR
PKSEISDEQY REFYKHVAHD FEDPLAWTHA RVEGRQEYTE LLYIPSRAPF DLWDRERKHG
VKLYVRRVFI MDDADKLMPL YLRFVKGVID SADLSLNVSR EILQGSKDID AIRAGCVKKV
LGVLEDLASN EADKYATFWQ AFGNVLKEGI GEDFANKDRI ARLLRFASTS NDSNVQNVSL
ADYVARMKDG QDKIYYITAD SFAAAKNSPH LEVFRKKGVE VLLLSDRVDE WVTGHLTEFD
GKALVSVAKG ELDLGQLEDE AEKEAQKQVE ETLQPLIERV GKALTEQVRE VRVTHRLTES
PACLVASEHG MSTHLERLLK SAGQEIEHQK PVLELNPAHP LVKKLDAEQS DTRFGELARV
LFDQALLAEG GQLDDPASFV RRVNSLMLEM AA
//
