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Database: UniProt
Entry: F7NJL5_9FIRM
LinkDB: F7NJL5_9FIRM
Original site: F7NJL5_9FIRM 
ID   F7NJL5_9FIRM            Unreviewed;      1001 AA.
AC   F7NJL5;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Chaperone protein {ECO:0000313|EMBL:EGO63769.1};
GN   ORFNames=ALO_11354 {ECO:0000313|EMBL:EGO63769.1};
OS   Acetonema longum DSM 6540.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Acetonema.
OX   NCBI_TaxID=1009370 {ECO:0000313|EMBL:EGO63769.1, ECO:0000313|Proteomes:UP000003240};
RN   [1] {ECO:0000313|EMBL:EGO63769.1, ECO:0000313|Proteomes:UP000003240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6540 {ECO:0000313|EMBL:EGO63769.1,
RC   ECO:0000313|Proteomes:UP000003240};
RX   PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA   Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA   Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA   Jensen G.J.;
RT   "Structural diversity of bacterial flagellar motors.";
RL   EMBO J. 30:2972-2981(2011).
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGO63769.1}.
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DR   EMBL; AFGF01000092; EGO63769.1; -; Genomic_DNA.
DR   RefSeq; WP_004095623.1; NZ_AFGF01000092.1.
DR   AlphaFoldDB; F7NJL5; -.
DR   STRING; 1009370.ALO_11354; -.
DR   eggNOG; COG0326; Bacteria.
DR   OrthoDB; 1837345at2; -.
DR   Proteomes; UP000003240; 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:0051082; F:unfolded protein binding; 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   PANTHER; PTHR11528:SF26; HEAT SHOCK PROTEIN (HSP90-FAMILY)-RELATED; 1.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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:UP000003240}.
SQ   SEQUENCE   1001 AA;  116166 MW;  532A61427EF2C0BF CRC64;
     MSKYHYKDKF GGEPNLVADV TKTALMIFLK RMNTQYFAKA LELREAVQKL LSYIPATFPH
     YTSHSVEHSD EIISQISQLL FKNQNSIKAT VNLSPTEAYI LIASAYLHDA GMVASDREKM
     EIIASERWKC WLSTEGPSKR FFEIEKLRND LFVEESIRQF LADRQLRFLI GEFIRKEHHI
     RSTQILQQNQ SELGRFAFDD PDLQRAISDV CLSHGLDYNE LDTDRYPDRR TIRGELVNMR
     FFAILLRVGD LLDTVNDRAC PLLINAASPL PADSFAHWSK YQRIVHRLTA PDRIEITARC
     KNQDEHRFLH DWFTWLVKEL KNAAISIIRC QLHNNWKPPV AEISTSSHPG NINIFPADDA
     LYIPMDWKFE FDTDLVFKRL ISDVYDSQSA FLRELIQNAL DATRCQVYID LKNCSLTLPK
     YPTEISETIR NKYPINIKLY EQEFTNELSG VREIKQVLSV EDFGIGMTEE IIQKYLLQVG
     KSYYTTEDFL RNYHFHPTSQ YGIGFLSVFG VSSKITLETY SPKKVGRPIS LNLAGPRSYI
     LVEKSDRNKN GTKITLVLDE PFETGDLEKI VRYWCKKVEF PIVLEDLGNQ ILITSEKPED
     FIYEIPEIIE PYGKYSIRCF PIQASGLEGE IYVFAHSTSE SESWADLNYA KNYIIDHPQA
     QIPTLPSDLT CIHGITIRHY NQLKNNCQLS IRVDFRDNSL KPSLSREKVR IPFRDENRLD
     PRIENRLVQI LSDHLQTTSL ASGNNEWIYK QRLIRNISFL EEFWNGIPRS IRMFLGGIPR
     LFSLKEIKSV EKIIAIVFPY EIENLKRRKF KLPEIAIPFN SLDSSVPVIT EIDMELLSKE
     HNKAIFDNRV ITNVSILPNG FLGVEWQLGI STIKLKDTIE LAFFDSSDFF GAVLHKTSDT
     VYSQIVLNEN NIFIQWLLNL KSMCESEDHG LSSRQFSHII DLVEKVVRYN DYPELLNHLN
     NWRNMGEISD QLDSLQVCSN EREFYISGKK MIVLNKYMLL M
//
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