ID E0IGG8_9BACL Unreviewed; 1121 AA.
AC E0IGG8;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=ATP-binding region ATPase domain protein {ECO:0000313|EMBL:EFM08468.1};
GN ORFNames=PaecuDRAFT_4761 {ECO:0000313|EMBL:EFM08468.1};
OS Paenibacillus curdlanolyticus YK9.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=717606 {ECO:0000313|EMBL:EFM08468.1, ECO:0000313|Proteomes:UP000005387};
RN [1] {ECO:0000313|EMBL:EFM08468.1, ECO:0000313|Proteomes:UP000005387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YK9 {ECO:0000313|EMBL:EFM08468.1,
RC ECO:0000313|Proteomes:UP000005387};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Anderson I.J.,
RA Johnson E., Loganathan U., Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RT "The draft genome of Paenibacillus curdlanolyticus YK9.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
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; AEDD01000017; EFM08468.1; -; Genomic_DNA.
DR AlphaFoldDB; E0IGG8; -.
DR STRING; 717606.PaecuDRAFT_4761; -.
DR eggNOG; COG0326; Bacteria.
DR eggNOG; COG3437; Bacteria.
DR eggNOG; COG5635; Bacteria.
DR Proteomes; UP000005387; Unassembled WGS sequence.
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:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:InterPro.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR007560; Restrct_endonuc_IV_Mrr.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR PANTHER; PTHR11528:SF41; HEAT SHOCK PROTEIN 90-6, MITOCHONDRIAL; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF04471; Mrr_cat; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:EFM08468.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000005387}.
FT DOMAIN 35..104
FT /note="Restriction endonuclease type IV Mrr"
FT /evidence="ECO:0000259|Pfam:PF04471"
FT COILED 248..275
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1121 AA; 130629 MW; 636B7D1CBBB59C49 CRC64;
MYERACSEAE IHDENNNCLN KPLAFEHQIG YPLCELQPRD FERLVFCLYH AEIQNQRTDA
YDEIQLMQGV GERGRDCLLL RAGKTVGLIQ CKRYKTNIDV SEIGKEIVKF VLHALLDPAL
LPDVNDFSYK VAVSYGFSEN ALKLMTSLTN QSYDKNVIQG WAVEVIAKNK GLATIVWDDV
KSSVFDTLDK MSFETIYPDT LNPLIESNSQ IKSMFFELKA VLDEKSFKEL LVEREKAALK
FYDAGLLERR LKEKNEALFH KLQETKQEAD RLFNAYSANF ILYSFHNKEH SVSVSELLGD
KVLDQGVLDA LNEAELYVLA SAAYLHDIGV CRTNEDIEQR FKAYEDSGQN HANKTVEEYA
REHHAFFTYD FISDHWEALK LDRSWKEAIA LVAGEKKDCD VYAFDYFDYA PAGGRTKVCI
PYLHTLLSIA DRLDVANLNA NYLLQHYQGM EEHKESKKLW EEMTYGISSR IVDEDRIVFE
GNCDNQLIYI SLNRHIQETK HQLEQLIAKV RKYKPQYKFS IHFIEEKIDT PFSQKWGFSI
DYNGIAETFM GKNIYEDKYD AIREAIQNAI DACQLRKAKE PTYVPEIEVR LTDKDIVIID
NGRGMDEYIV QNYFSKLCKS YYKDFEIDSI GQFGIGVFSY FMLCDSFSVE TKTREGQRLC
FKGNKNLYSY FYFYDEGKLN IAEGTALTLH LKEEVLREIN VETLVTKVRD RFRFVDIPIK
VVSEDTSTVM TRDSFSLDLE AELMYEVDYI NRDKIKDLLL LESHINNERF EGTCGIIVER
SDNALGYKPF NFTRTLHTVS SSYEGKVLIC QKGVKVIERQ YKYLRRASKL LDQLICSINI
KQNLKINIGR NEFIDDQLDA IIAEFESDLL HKFFGSIHQF DNKESYEVCS EFVDYYLEPY
LFPNKRLEDF TYNHFYIKAY IGKSEAYMLL NDFITEHPSF IFIGGASKFN KRAIRVAIRT
GIPVMFIEND GLCRFYYQYF EEMNYAFSIY GHLNDLLMIT KTEEAHEKYP IHYGMGISIN
NQLLFEVVSN IYFARAYYNT NHPLIQFYVT NRNKIKDNDK LFDKFHRFFK FLSNLYGSVT
TTISLHQVNE LLAEILSSFN VSIQLTAEDF PERFRGNLLV D
//