ID   HTPG_ANAMM              Reviewed;         638 AA.
AC   Q5PB86;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=AM376;
OS   Anaplasma marginale (strain St. Maries).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma.
OX   NCBI_TaxID=234826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=St. Maries;
RX   PubMed=15618402; DOI=10.1073/pnas.0406656102;
RA   Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L.,
RA   Palmer G.H., McGuire T.C., Knowles D.P. Jr.;
RT   "Complete genome sequencing of Anaplasma marginale reveals that the surface
RT   is skewed to two superfamilies of outer membrane proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005).
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; CP000030; AAV86443.1; -; Genomic_DNA.
DR   RefSeq; WP_010263346.1; NZ_AFMU01000022.1.
DR   AlphaFoldDB; Q5PB86; -.
DR   SMR; Q5PB86; -.
DR   PRIDE; Q5PB86; -.
DR   GeneID; 7398387; -.
DR   KEGG; ama:AM376; -.
DR   PATRIC; fig|320483.3.peg.316; -.
DR   HOGENOM; CLU_006684_3_0_5; -.
DR   OMA; MRRMKEM; -.
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; PF02518; HATPase_c; 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; Stress response.
FT   CHAIN           1..638
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000224194"
FT   REGION          1..328
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          329..558
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          484..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          559..638
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   638 AA;  72356 MW;  8A77EE1197057F32 CRC64;
     MGDVEELKFS AEVGKVLSLV VHSLYTNKDI FLREVISNAS DACDKLRYLF CSDQSLMEAG
     EELRIVISVD RDRRELTVRD NGIGMSRKEL IDNLGTIASS GTQRFLEEFK GGKAQGCDLI
     GKFGVGFYSV FMVATDVVVE SCKAGEKVGH RWQSSGDGVF SVSTIEGDVS RGTKVILTLR
     EDEFDFLDKF RIEHIVTTYS DHVGYPIYLI ASDGTEEKLN SGVAIWTKPK DEISESEHME
     FFRSISHIGS NPWMVIHNKN EGTIEYINLL YVPSVKPFDL FHPDRRCSVK LYVNRVFITE
     DNVQVIPQYM RFLRGVIDSS DLPLNISRET LQNNMVIEKI KASVTRRVLT SLREKADSDP
     VSYKTFWENF GPVLKEGLCE AMDTESRESI LSVCRFYSSN SKEGELISLG DYISRMKPGQ
     EHIFYLSGND LESAMRSPQI EGMVSNGIEV VLLVDPVDDF WTSVVLEYKG VPFKSVTRVD
     ESDLEKFTEG DDQQSTKKKK EKKDTDDAQQ KENVEAFIDY MKKVLGDSVS DIKVSRKLTT
     SLVCLAVPEH ALDIRMERFL REQKQLSYKG SRILELNIKH PVLSGLLREY KDNGESELLE
     NMVHVLFDQA CIIEGEEVNS AVDFANRMNQ VLARLFKK