ID A0A1Z1WSM4_9ACTN Unreviewed; 639 AA.
AC A0A1Z1WSM4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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 ECO:0000313|EMBL:ARX89443.1};
GN ORFNames=SMD44_08930 {ECO:0000313|EMBL:ARX89443.1};
OS Streptomyces alboflavus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67267 {ECO:0000313|EMBL:ARX89443.1, ECO:0000313|Proteomes:UP000195880};
RN [1] {ECO:0000313|EMBL:ARX89443.1, ECO:0000313|Proteomes:UP000195880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MDJK44 {ECO:0000313|EMBL:ARX89443.1,
RC ECO:0000313|Proteomes:UP000195880};
RA Wang Y., Du B., Ding Y., Liu H., Hou Q., Liu K., Wang C., Yao L.;
RT "Streptomyces alboflavus Genome sequencing and assembly.";
RL Submitted (MAY-2017) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00505}.
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DR EMBL; CP021748; ARX89443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z1WSM4; -.
DR KEGG; salf:SMD44_08930; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000195880; 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:UP000195880};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505,
KW ECO:0000313|EMBL:ARX89443.1}.
FT DOMAIN 28..186
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..344
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 562..639
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 639 AA; 71496 MW; 83A45E27DECEDF7B CRC64;
MASSVETLEF QAETRQLLRL VIHSIYSNKD IFLRELISNA SDALDKLRLA SLTDADITEN
GTADLHISLE VDKDARTLTV RDNGIGMTRD ELVELIGTIA KSGTASLLEK IKESQDAATA
ESLIGQFGVG FYSAFMVADK VTVRTRRAGT DSGTQWESDG ENSYTVQAAD DLPVGTSVTL
HLKPADSEDG LADYLSEPKI RQIVKRYSDF IRWPIRMTTD RTDADGAITT DLDTLNSMKA
LWARPRSEVS EDEYHEFYQQ ISHDWLPPAE TIHMRAEGTF EYEALLFIPS QAPFDLYSRE
SKSGVQLYVK RVFIMDDCEA LMPHYLRFVK GVVDAHDLSL NVSRELLQHD RQIQGVRRRL
IKKVLGAIKD MQAKDAERYS KVWAQFGRAL KEGLLEDPDN TEVLLELVSA ASTHDPEKTT
TLREYVERMK DGQDTIYYLT GESRAMVENS PHMEAFAAKG YEVLILTDPI DEVWVDQVPA
FDGHRLQSIA KGQVDLDETA DGENETDTDK AQREQDFAVL LPWLTTTLSD HVKQVRLSSR
LTTSAACIVG DAHDVTPTLE KMYRAMGQQI PTVKRILELN PTHPLITALR TAHHANAEAP
ALTEIAELIY GSALLAEGGD LPDPARFTRL LTDHLTRTL
//
