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HTPG_MYCA1
ID   HTPG_MYCA1              Reviewed;         644 AA.
AC   A0QEJ0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=MAV_2118;
OS   Mycobacterium avium (strain 104).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=243243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000479; ABK65022.1; -; Genomic_DNA.
DR   RefSeq; WP_009976349.1; NC_008595.1.
DR   AlphaFoldDB; A0QEJ0; -.
DR   SMR; A0QEJ0; -.
DR   EnsemblBacteria; ABK65022; ABK65022; MAV_2118.
DR   KEGG; mav:MAV_2118; -.
DR   HOGENOM; CLU_006684_3_0_11; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000001574; 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; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Stress response.
FT   CHAIN           1..644
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000014930"
FT   REGION          1..352
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          353..566
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          567..644
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   644 AA;  72840 MW;  DF619B0DA99E9457 CRC64;
     MNARVEQLEF QAEARQLLDL MVHSVYSNKD SFLRELISNA SDALDKLRLE AFRNKDLDVD
     TSDLHIQIEV DKDARTLTIR DNGIGMTRAE VVDLIGTLAK SGTAELRQQL REAKNAQNEA
     ASEELIGQFG IGFYSSFMVA DKVELLTRKA GESEATKWES SGEGTYTIES VENAPQGTSV
     TLHLKPEDTE DELHDYTSEF KIKSLVKKYS DFIAWPIRME VERRTPATEE GGEETVTREV
     ETLNSMKALW ARPKDEVSEE EYKEFYKHIA HAWDDPLEVI AMKAEGTFEY QALLFIPSHA
     PFDLFNRDAH TGIQLYVKRV FIMGDCDQLM PEYLRFVKGV VDAQDMSLNV SREILQQDRQ
     IKAIRRRLTK KVLSTIKELQ SERPDDYRTF WTQFGRVVKE GLLSDFDNQE TLLQLCSFAS
     THSEEEATTL AQYVERMKEG QTQIFYATGE TRQQILKSPH LEAFKAKGYE VLLLTDPVDE
     VWVGTVTEFD GKPLQSIAKG EVDLSAEGEE SQAEREEQQK EFADLLAWLK DTLSDHVKEV
     RLSNRLTDSP ACLITDAFGI TPALARLYRA SGQDIPVGKR ILELNPKHPL VTGLRQAHQD
     RADDPSVAET AELLYGTALL AEGGALDDPA RFAEILADRL ARTL
 
 
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