ID A0A0S7BAV8_9CHLR Unreviewed; 619 AA.
AC A0A0S7BAV8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=LARV_02623 {ECO:0000313|EMBL:GAP14847.1};
OS Longilinea arvoryzae.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Longilinea.
OX NCBI_TaxID=360412 {ECO:0000313|EMBL:GAP14847.1};
RN [1] {ECO:0000313|EMBL:GAP14847.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KOME-1 {ECO:0000313|EMBL:GAP14847.1};
RA Sekiguchi Y., Ohashi A., Matsuura N., Tourlousse M.D.;
RT "Draft Genome Sequences of Anaerolinea thermolimosa IMO-1, Bellilinea
RT caldifistulae GOMI-1, Leptolinea tardivitalis YMTK-2, Levilinea
RT saccharolytica KIBI-1,Longilinea arvoryzae KOME-1, Previously Described as
RT Members of the Anaerolineaceae (Chloroflexi).";
RL Submitted (JUL-2015) 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}.
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DR EMBL; DF967972; GAP14847.1; -; Genomic_DNA.
DR RefSeq; WP_075074074.1; NZ_DF967972.1.
DR AlphaFoldDB; A0A0S7BAV8; -.
DR STRING; 360412.LARV_02623; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000055060; 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: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 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:UP000055060};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT REGION 1..328
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 329..544
FT /note="B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 545..619
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 619 AA; 70065 MW; 5D694A5C16917CEE CRC64;
MSDMNSNNPV PFKAETHQLL EILIHSLYTE REVFLRELIS NASDALTRLN FETLTKREIQ
DPELELGIWI TADPDAKTLT IRDTGLGMTA AELAENLGTI AHSGARAFLE AARSGEAKVE
DIIGQFGVGF YSAFMVADWI RVTSRSFQPE AAPAVWFSTG ADTFTVGPAE KNERGTEVIL
RVKDEYLEFC KEERIRQIIK RHSDFVPFPI YVGENKEQAN RQTALWRQQP RQVQEKDYQD
YYRQLTLEFE PPLSWLHLSV DAPVQVYALL YIPASAEPGI VSTRKTDGLR LYARKVLIQE
YCKDLLPQYL RFMAGVVDSE DLPLNVSRES VQSNRTMGQL KKLLTSKVLD HFASLAKDHS
DTYTKFWTVY GSFLKEGIAT PKENSEPLLP LLRFHSLNHP QDWISFDQYL DNIPAEQNQI
YYLLGDSEMA ALHSPHLEAF RSRGLDVLIL ADPIDSFALL NVTQYRDHTL ADAATADLPA
APEKTEKPAE AEKLMDEAQS ESILQRFKTV LTDRISDARL SDRLVESPVR LVQPKEGPSA
EIQRVYRILQ KDLDTPKPVL EINPSHPIIQ ALARLGQDDV SASLMVEQIF ANAQIMEGLP
VEPSQMVDRI QQIILKALK
//