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Database: UniProt
Entry: F8E5E7_FLESM
LinkDB: F8E5E7_FLESM
Original site: F8E5E7_FLESM 
ID   F8E5E7_FLESM            Unreviewed;       626 AA.
AC   F8E5E7;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 65.
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   OrderedLocusNames=Flexsi_2084 {ECO:0000313|EMBL:AEI15710.1};
OS   Flexistipes sinusarabici (strain ATCC 49648 / DSM 4947 / MAS 10).
OC   Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC   Flexistipitaceae; Flexistipes.
OX   NCBI_TaxID=717231 {ECO:0000313|EMBL:AEI15710.1, ECO:0000313|Proteomes:UP000006621};
RN   [1] {ECO:0000313|EMBL:AEI15710.1, ECO:0000313|Proteomes:UP000006621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4947 / MAS 10 {ECO:0000313|Proteomes:UP000006621};
RX   PubMed=22180813; DOI=10.4056/sigs.2235024;
RA   Lapidus A., Chertkov O., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA   Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Pagani I., Ivanova N., Huntemann M., Mavromatis K., Mikhailova N., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Rohde M.,
RA   Abt B., Spring S., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Woyke T.;
RT   "Genome sequence of the moderately thermophilic halophile Flexistipes
RT   sinusarabici strain (MAS10).";
RL   Stand. Genomic Sci. 5:86-96(2011).
RN   [2] {ECO:0000313|Proteomes:UP000006621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4947 / MAS 10 {ECO:0000313|Proteomes:UP000006621};
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Chertkov O.,
RA   Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Flexistipes sinusarabici DSM 4947.";
RL   Submitted (JUN-2011) 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; CP002858; AEI15710.1; -; Genomic_DNA.
DR   RefSeq; WP_013887158.1; NC_015672.1.
DR   AlphaFoldDB; F8E5E7; -.
DR   STRING; 717231.Flexsi_2084; -.
DR   KEGG; fsi:Flexsi_2084; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_0; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 9802640at2; -.
DR   Proteomes; UP000006621; 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; 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; 2.
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.
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:UP000006621};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT   REGION          1..334
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT   REGION          547..626
FT                   /note="C"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   626 AA;  71616 MW;  304E12A2B0EBF5F9 CRC64;
     MAETVQFQAE VKELLNLVIN SLYTHKEIFL RELISNASDA IDKAKYLSIT DKSNNLAGTE
     WKIKIKPDKD EGTITISDNG IGLSRDEAVK SLGTIAHSGT KEFINAVKSG QIKEQPELIG
     QFGVGFYSAF MVADKITVIS KKVGEEKGVK WESAADGTFT VDDADKENFG TDVTVTLKKD
     EREFLDEWRI KEIVKKYSDY IEYPITMDVE KEDKDGNKSV EEETLNSMKA LWLKDKSEIT
     ENEYNEFYKH ISHDFTDPLE TIHFKAEGTQ EFSALLYIPS HAPFDIFYKD FKFGPALYVK
     KVQIMDHCEE LMPPYLRFIK GVVDSSDLPL NVSREILQNN RKVEVIKKNI TKKVLETLKK
     VKENDSEKYD KFIGEFGKIL KEGIHYDFSR KEEIAGLLTF HTTKTAANEK IDFDKYLENM
     KEEQKEIYYI CGDSVDEVKN SPYLERFKDK DVEVIFFTDE IDDMIMSTLG EYKGKTLKSV
     LKGDISLDEE EKKETENREK ELKGFLDSIK DHLKGKVKDV KISNRLKDSP ACLVVDEDAM
     DPAMKKLLES MGQEVPSQEK TLEINAEHPV VKQLKEIYET DPNSGTVSDY TDLLYNLSLV
     VEGEKPENPS DFVKKLSEMM SKSLKS
//
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