ID A9GDV2_SORC5 Unreviewed; 662 AA.
AC A9GDV2;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 91.
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=sce9231 {ECO:0000313|EMBL:CAN99404.1};
OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS ce56)).
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=448385 {ECO:0000313|EMBL:CAN99404.1, ECO:0000313|Proteomes:UP000002139};
RN [1] {ECO:0000313|EMBL:CAN99404.1, ECO:0000313|Proteomes:UP000002139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139};
RX PubMed=17965706; DOI=10.1038/nbt1354;
RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA Puehler A., Mueller R.;
RT "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL Nat. Biotechnol. 25:1281-1289(2007).
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; AM746676; CAN99404.1; -; Genomic_DNA.
DR RefSeq; WP_012241839.1; NC_010162.1.
DR AlphaFoldDB; A9GDV2; -.
DR STRING; 448385.sce9231; -.
DR KEGG; scl:sce9231; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_7; -.
DR BioCyc; SCEL448385:SCE_RS47215-MONOMER; -.
DR Proteomes; UP000002139; 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; 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.
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:UP000002139};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 65..226
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..367
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..662
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 73274 MW; 28A7360A902C4306 CRC64;
MNTESPNPET SGSTPSAEPS GAAPGPETPA STPSEEAKAA GAVELPFQAE VQQVLALVIN
SLYANQEVFL RELISNASDA LDKARFLALT REGVAEQAGE PAILITLDDA ARTLTIEDNG
IGMTRDEVVQ NLGTIARSGS LEFLKANAEA AKQKKDGGKL QLIGQFGVGF YAAFMVASRV
DVQTRSMLPG AEPVLWRSSG AGSFTVAPGD REHPGTKIVL HLKDDAREYT KVWRIKEIIR
KYSDFVHFPI KVNDEVANRS AALWTLPKSQ ITEEQHAEFF RHVTGGYEGE KPLLTVHLSI
DAPVQFHALL YVPEKAPADM FHKDRRGVRL YAKRVLIVED CDKLTPMYLR FLRGVVDSED
LSLNVSREML QENRTLSQIE QQIVKQVLKS LKDLSESEPE RYAAFWKEFG RVIKEGVTND
WKNKDAIAEL CRFESMNTEA GKVISLRDYV AKMPEAQKEI YYVTGLGRHA VEQSPHLEAF
RKRGYDVLFL VDPVDEWFVQ SLNEFDKRRL KSVMHGDVDL GAEPEKKDEP EASVDAAVAA
VKAALGERVK DVRVSRRLTD SASCLVAAEG DPGANFERIM KLIDQNTGES KRILELNPGH
PVVKNLNILA GREPGSERVK QWSELLLDQA LLVEGVVQEP AKLVRRIQDL LAQVSSAAVS
QS
//
