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Database: UniProt
Entry: L0KK92_MESAW
LinkDB: L0KK92_MESAW
Original site: L0KK92_MESAW 
ID   L0KK92_MESAW            Unreviewed;       630 AA.
AC   L0KK92;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 62.
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=Mesau_03085 {ECO:0000313|EMBL:AGB45461.1};
OS   Mesorhizobium australicum (strain HAMBI 3006 / LMG 24608 / WSM2073).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=754035 {ECO:0000313|EMBL:AGB45461.1, ECO:0000313|Proteomes:UP000010998};
RN   [1] {ECO:0000313|Proteomes:UP000010998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 24608 / HAMBI 3006 / WSM2073
RC   {ECO:0000313|Proteomes:UP000010998};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Gu W., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Reeve W.G., Howieson J.G., Tiwari R.P.,
RA   O'Hara G.W., Atkins C.A., Ronson C.W., Nandasena K.G., Woyke T.;
RT   "Complete sequence of Mesorhizobium australicum WSM2073.";
RL   Submitted (FEB-2012) 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; CP003358; AGB45461.1; -; Genomic_DNA.
DR   RefSeq; WP_015316884.1; NC_019973.1.
DR   AlphaFoldDB; L0KK92; -.
DR   STRING; 754035.Mesau_03085; -.
DR   KEGG; mam:Mesau_03085; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_5; -.
DR   OrthoDB; 9802640at2; -.
DR   Proteomes; UP000010998; 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:UP000010998};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_00505}.
FT   DOMAIN          31..190
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          1..335
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT   REGION          336..551
FT                   /note="B"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT   REGION          552..630
FT                   /note="C"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   630 AA;  69550 MW;  A460CFE28A6AEEEF CRC64;
     MTTDTKATET KAFEADVSRL LHMMVHSVYS DKDVFLRELI SNAADACEKL RFEAVSRPEL
     LADDPKPRIS ISADPDGKLI TVEDNGIGMS RDDMTEALGT IARSGTRAFI ERVGAGNSSE
     DTQLIGQFGV GFYSAFMVAT RVDVISRLAG SEEAWRWSSD GKGSYEIAPA PLEAAPKRGT
     RVVLHLMDDA VSYTGSYRLE QLAKSQSGHV PVPITLIERP GAEARDIADG TALWVRPKSE
     IKPEEYTDFY RGVSGQYDEP AATIHFRAEG RQEYSVLAFV PGSRPFDLFD QDRKGRMKLY
     VRRVFITDDA DLLPRYLRFM RGLVDSADLP LNVSREMIQE SPLLAAIRKG LTNRVLGDLA
     KLAENETEAY AKIWENFGVV LKEGLYEDHE RREQLLKLAR FRSTASGEGW RGLAEYVSAM
     KEGQKAIFFM AGDDRARLEA SPQLEGFKAR GIEVLLLTDP VDSFWTSMAP EFDGKPFRSV
     TQGVAELSEI PLLDEANKPD AAAAPEVDGF LAFLKAALGD AVSDVKASDR LTESAVCLVA
     PEHGPDRQFE RLLNAAGRLD KTAKPILEIN PRHQRVLALA SLGEDEQAFK EDAAHLLYDE
     ARVLDGDKPA DARAFSERLA RLIARGISKG
//
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