ID A3PCV6_PROM0 Unreviewed; 634 AA.
AC A3PCV6;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Heat shock protein HtpG {ECO:0000313|EMBL:ABO17581.1};
GN Name=htpG {ECO:0000313|EMBL:ABO17581.1};
GN OrderedLocusNames=P9301_09581 {ECO:0000313|EMBL:ABO17581.1};
OS Prochlorococcus marinus (strain MIT 9301).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=167546 {ECO:0000313|EMBL:ABO17581.1, ECO:0000313|Proteomes:UP000001430};
RN [1] {ECO:0000313|EMBL:ABO17581.1, ECO:0000313|Proteomes:UP000001430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9301 {ECO:0000313|EMBL:ABO17581.1,
RC ECO:0000313|Proteomes:UP000001430};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000576; ABO17581.1; -; Genomic_DNA.
DR RefSeq; WP_011862929.1; NC_009091.1.
DR AlphaFoldDB; A3PCV6; -.
DR STRING; 167546.P9301_09581; -.
DR KEGG; pmg:P9301_09581; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_2_3; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000001430; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:InterPro.
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 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 SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001430};
KW Stress response {ECO:0000313|EMBL:ABO17581.1}.
SQ SEQUENCE 634 AA; 72445 MW; 1A210D7D2314D155 CRC64;
MEKGEIRINT ENIFPIIKKA VYSDHEIFLR ELVSNGVDAI SKRRMASMAG DCENTEEAQV
KITINREKNT LTISDNGIGM NDEEIKKYIN QVAFSSAEEF LTKYKKDNDE FIGHFGLGFY
SSFMVADKVD ILTKSAIGES KAFKWSCDGS PNFTLEESER ETIGTDVILH LLEEEKEFIE
PERIKSLIKK YCDFMPIDVL LEGETINKKN PPWRKQPSEL KDEDYIELYK YLYPFQGDPL
LWIHLNTDYP YDIQGILYFP KLSGRADWEK GEIKLFCNQV FVSDSIKEIV PKYLLPLRGV
IDSTDIPLNV SRSALQTDRK VRSISSFISK KIANKLKDLI KNSPEFYAEI WDSISAFIKI
GAIEDEKFAE LVNNSIIFET IINSEKNVTK NIENKSLIKS NDKYFTTLAN YKERNKLTDS
KKIIYCSDLI AQSSALKICL SDNKEVIKSD PLIDAQFLPW LESKNEDFQF QRVDSEINEI
EDKESKEIVD KDGKSNTDNL RDTIVKALNN EKVTVKVQSL SSKDAPPAMI LLPEQMRRIN
DMGAYMEQKM PGLPEYHVLL INKEHPLIVG LNKITGNKII IDEKDPTENP LASKIANHVY
DMAKLSVGGL DQEQIINLQN NNAELISELL NSTN
//
