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HTPG_NEOSM
ID   HTPG_NEOSM              Reviewed;         620 AA.
AC   Q2GDR7;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Chaperone protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE   AltName: Full=Heat shock protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE   AltName: Full=High temperature protein G {ECO:0000255|HAMAP-Rule:MF_00505};
GN   Name=htpG {ECO:0000255|HAMAP-Rule:MF_00505}; OrderedLocusNames=NSE_0495;
OS   Neorickettsia sennetsu (strain ATCC VR-367 / Miyayama) (Ehrlichia
OS   sennetsu).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Neorickettsia.
OX   NCBI_TaxID=222891;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-367 / Miyayama;
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA   Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C.,
RA   Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C.,
RA   Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D.,
RA   Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA   Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(2006).
CC   -!- FUNCTION: Molecular chaperone. Has ATPase activity. {ECO:0000255|HAMAP-
CC       Rule:MF_00505}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00505}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00505}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00505}.
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DR   EMBL; CP000237; ABD46211.1; -; Genomic_DNA.
DR   RefSeq; WP_011451885.1; NC_007798.1.
DR   AlphaFoldDB; Q2GDR7; -.
DR   SMR; Q2GDR7; -.
DR   STRING; 222891.NSE_0495; -.
DR   EnsemblBacteria; ABD46211; ABD46211; NSE_0495.
DR   KEGG; nse:NSE_0495; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_5; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000001942; 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:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.790; -; 1.
DR   Gene3D; 3.30.565.10; -; 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_S5_D2-typ_fold.
DR   PANTHER; PTHR11528; PTHR11528; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF110942; SSF110942; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..620
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000236998"
FT   REGION          1..328
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          329..547
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          548..620
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   620 AA;  71307 MW;  4863E71FBEDD04BB CRC64;
     MEKTEHKNTY SFDADASKVL NLVIHSLYRH KDVFLRELIS NASDALNKLR EASYFDQELL
     EDNPELEILI SLNKEKKILE ISDNGIGMDE KELVENLGTV ARSGTEKFLE SLKDKKVDLI
     GQFGVGFYSV FMVADKVEVE TRKAGTKKGY IWGSRGRDSF YVDELGESVS RGTKIRIYLK
     DNSEEFLDKF KLEHVVVTNS NHIAFPIYLI DEKGEKDQIN SASAIWTKNK TEITDEEHQN
     FFRDVAHVGG KPWMIIHNKN EGSTEYINLL YVPSIKPFDL YNPDRRASVK LYIKKVFITE
     ENVQLIPQYL RFLKGVVDCA DLPLNISRET LQYNNALVKI KKSLTNRVLN ELKKRADSNP
     EEYISGFWNN FGAVLKEGLC EAMPTDERER LFALCRFYSL KKEKLISLDE YIQDMHPEQK
     EIYCLCSTSF ESAKNSPQLE GFVSRGLDVL FFTDPVDDFW ISVSHEYKSY NIKSITRSSI
     DLDAFAELEK AGQEVQQHHD KEIDRLIAKM QEVLKDEVES VRISKRLTES PVCLAVPDGA
     MDIRMEKFML EQKQLHSRSK KILEINASHP VIGKIIGKVD SPEVEDLIFL LYDQACILQG
     DEVRNPVRMS KALTRLLLMT
 
 
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