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