ID A2C227_PROM1 Unreviewed; 634 AA.
AC A2C227;
DT 20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 20-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Heat shock protein HtpG {ECO:0000313|EMBL:ABM75537.1};
GN Name=htpG {ECO:0000313|EMBL:ABM75537.1};
GN OrderedLocusNames=NATL1_09791 {ECO:0000313|EMBL:ABM75537.1};
OS Prochlorococcus marinus (strain NATL1A).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=167555 {ECO:0000313|EMBL:ABM75537.1, ECO:0000313|Proteomes:UP000002592};
RN [1] {ECO:0000313|Proteomes:UP000002592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL1A {ECO:0000313|Proteomes:UP000002592};
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}.
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DR EMBL; CP000553; ABM75537.1; -; Genomic_DNA.
DR RefSeq; WP_011823663.1; NC_008819.1.
DR AlphaFoldDB; A2C227; -.
DR KEGG; pme:NATL1_09791; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_2_3; -.
DR Proteomes; UP000002592; 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; 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_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.
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 Stress response {ECO:0000313|EMBL:ABM75537.1}.
FT DOMAIN 27..178
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
SQ SEQUENCE 634 AA; 72203 MW; 7ED0332DAF394267 CRC64;
MSVKEEGTIL IHTENIFPII KKAVYSDHEI FIRELISNSV DAIKKRKMAA FAGDCVAADD
EKIKISIDRE HKTLTISDNG IGMTSDEIKK YINQVAFSSA EEFLEKYKQP DDGFIGHFGL
GFYSSFMVAE EVEIITKSAK NDSQAIQWKC NGSPQYSLDE SDKEEVGTDI ILHLMEDEIE
YIEPSRIKTL IKKYCDFMPI EISLEEEVIN KMNPPWRESK QNLKDEDYIE LYKYLYPFQG
DPLLWVHLNT DYPYNLQGIL YFPKISGRAD WESGEIKLFC NQVFVSDSIK EIVPRYLLPL
RGVIDSPDIP LNVSRSALQS DRRVKSIGNF IAKKLADKLK TLKKDETQFY ADIWDSIAPF
IKIGAMEDEK FAEQVKDIIL YSTTKVPVED NEENNELVKS GSKTFTTLEG YKNRLTDENK
KILYSTDEVS QSTALNMWTS QGKEVLKLDT VIDTQFIPWL EEKNKEINFV RVDSELDENI
KDDSPEIADK DGNTKSETLK KIISSALNNE KVTVQIQNLK GDNSPPSLIL LPEQMRRIND
ITALMEQKLP GLPEYHNLIV NSNHPLIQGL LKLNSNQIVI EGSSKSEEGQ LASDIAIHVY
EMAKLSIGGL ENKDIAAFQN RNAELLGKLM KNFV
//
