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Database: UniProt
Entry: A0A0P0SHV8_9PSEU
LinkDB: A0A0P0SHV8_9PSEU
Original site: A0A0P0SHV8_9PSEU 
ID   A0A0P0SHV8_9PSEU        Unreviewed;       609 AA.
AC   A0A0P0SHV8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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   ORFNames=AD017_01980 {ECO:0000313|EMBL:ALL84185.1};
OS   Pseudonocardia sp. EC080619-01.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL84185.1, ECO:0000313|Proteomes:UP000066228};
RN   [1] {ECO:0000313|EMBL:ALL84185.1, ECO:0000313|Proteomes:UP000066228}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL84185.1,
RC   ECO:0000313|Proteomes:UP000066228};
RX   PubMed=26535611; DOI=10.1021/jacs.5b09794;
RA   Van Arnam E.B., Sit C.S.;
RT   "A Rebeccamycin Analog Provides Plasmid-Encoded Niche Defense.";
RL   J. Am. Chem. Soc. 137:14272-14274(2015).
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; CP012184; ALL84185.1; -; Genomic_DNA.
DR   RefSeq; WP_060576185.1; NZ_CP012184.1.
DR   AlphaFoldDB; A0A0P0SHV8; -.
DR   STRING; 1096856.AD017_01980; -.
DR   KEGG; pecq:AD017_01980; -.
DR   PATRIC; fig|1096856.3.peg.417; -.
DR   Proteomes; UP000066228; 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:UP000066228};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_00505,
KW   ECO:0000313|EMBL:ALL84185.1}.
FT   DOMAIN          8..165
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          1..322
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT   REGION          535..609
FT                   /note="C"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   609 AA;  67621 MW;  4CAA7A52145DA58E CRC64;
     MIHSIYSNKD VFLRELISNA SDALDKVRLA AYQDKELGAE TDDLHVELVA DPGARTLTVR
     DNGIGMTRDE VVELIGTIAK SGTAELLAKL QDAGDGDQAR DLIGQFGVGF YSSFMVADRV
     ELTTRKAGTG GGVRWESDGE GSYTIADVDD APQGTAVTLH LKASDAEDQM HDYADPGVLR
     RIVKTYSDFI TWPVRMTPEQ TPDTESEPEP ETLNSMKALW ARPQKDVSDE EYAEFYRHVS
     HDWQEPLETM RLAAEGTFEY QALLFLPQVA PMDLYMRDAR RGVQLYVRRV FIMDDCEALV
     PEYLRFVKGV VDAADLSLNV SREILQQDRQ ISAIRRRLVK KVLSTIGTLR DEQPEKYATF
     WEQFGRALKE GLLSDADNTE TILGVSSFAS THATDGPTTL AAYTERMQEG QDAIYYMTGD
     SASSIQSSPH MEAFRDKGYE VLLLTDPVDE VWVDGVEGFD GTPFRSIAKG QVDLQSDEDK
     EKAEEQRTEF AGLCEWMTGV LEEEVKEVRL SSRLTTSPAV LVGDEFDMTP TLEKMYRAMG
     QEPPKVKRIL ELNPSHPLVT GLRDAQAAGT DASETAELLH GMALLAEGGE LADPSRFVGL
     LAGRLERTL
//
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