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Database: UniProt
Entry: A0A1M6HN24_9BACT
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ID   A0A1M6HN24_9BACT        Unreviewed;       615 AA.
AC   A0A1M6HN24;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=SAMN02745181_1519 {ECO:0000313|EMBL:SHJ23569.1};
OS   Rubritalea squalenifaciens DSM 18772.
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC   Rubritaleaceae; Rubritalea.
OX   NCBI_TaxID=1123071 {ECO:0000313|EMBL:SHJ23569.1, ECO:0000313|Proteomes:UP000184510};
RN   [1] {ECO:0000313|EMBL:SHJ23569.1, ECO:0000313|Proteomes:UP000184510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18772 {ECO:0000313|EMBL:SHJ23569.1,
RC   ECO:0000313|Proteomes:UP000184510};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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       Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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; FQYR01000003; SHJ23569.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M6HN24; -.
DR   STRING; 1123071.SAMN02745181_1519; -.
DR   InParanoid; A0A1M6HN24; -.
DR   OrthoDB; 9802640at2; -.
DR   Proteomes; UP000184510; 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; IPR036890; HATPase_C_sf.
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:SF44; HEAT SHOCK PROTEIN 75 KDA, MITOCHONDRIAL-RELATED; 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   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.
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:UP000184510};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT   REGION          1..325
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT   REGION          538..615
FT                   /note="C"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   615 AA;  69195 MW;  11C73DFFE2D195E2 CRC64;
     MSTAEVQQHG FQAEVKQLLD IVIHSLYTDR EIFIRELVSN ASDALEKLRL KQLTEKGIYK
     ADLPLEITIT TDEDAKTLTI ADHGIGMTRE ELQQNLGTIA HSGTKAFLEQ LKEKGENNAD
     VIGKFGVGFY SAFMAADEVE VYTHSWQEDA ENLKWTSDGA SGYSVEAVDE QARGCKIVIK
     LKEGQEEFAK AERVKEILEK YSNFVTFPIN LNGERVNKVE ALWMKSKSDV TEEEYKEFYK
     FVSHAWDEPT YTMHFSADAP LAINSLLFVP GENQEQFGMG QMEPGVALYC RKVLIDPKPS
     KLLPEWLRFL RGVIDSEDLP LNISRESMQD SALIQKLNKL ITKRFLKFLE RQAKDDTEKY
     EGFYKKFSRF LKEGIATSFE HQEQLAGLLR FESTMTDAGK LTSMSEYLDR AKDGQEEIYY
     LVGNSRELLE KGPYLEAFKA RGLEVILFTD GVDQYVMDAL PEFKGKKFVA ADRADIDLED
     MDAEGEALDE ASLKGLTDWL GETLGERVEK VEAGKRLVNS PVAALAPKEA PNAQMRAMMK
     AMGQELPEPK VTLEVNPRSE VIKNLAGLKD RDTELAGIVA QQLTDNALLA AGLLENPQEM
     VGRLNDLLSR VSSEK
//
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