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Database: UniProt
Entry: E0IGG8_9BACL
LinkDB: E0IGG8_9BACL
Original site: E0IGG8_9BACL 
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}.
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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
//
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