LON_AYWBP
ID LON_AYWBP Reviewed; 791 AA.
AC Q2NJE3;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Lon protease {ECO:0000255|HAMAP-Rule:MF_01973};
DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_01973};
DE AltName: Full=ATP-dependent protease La {ECO:0000255|HAMAP-Rule:MF_01973};
GN Name=lon {ECO:0000255|HAMAP-Rule:MF_01973}; OrderedLocusNames=AYWB_333;
OS Aster yellows witches'-broom phytoplasma (strain AYWB).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX NCBI_TaxID=322098;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AYWB;
RX PubMed=16672622; DOI=10.1128/jb.188.10.3682-3696.2006;
RA Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A., Shevchenko D.V.,
RA Tsukerman K., Walunas T., Lapidus A., Campbell J.W., Hogenhout S.A.;
RT "Living with genome instability: the adaptation of phytoplasmas to diverse
RT environments of their insect and plant hosts.";
RL J. Bacteriol. 188:3682-3696(2006).
CC -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC degradation of mutant and abnormal proteins as well as certain short-
CC lived regulatory proteins. Required for cellular homeostasis and for
CC survival from DNA damage and developmental changes induced by stress.
CC Degrades polypeptides processively to yield small peptide fragments
CC that are 5 to 10 amino acids long. Binds to DNA in a double-stranded,
CC site-specific manner. {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01973};
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- INDUCTION: By heat shock. {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_01973}.
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DR EMBL; CP000061; ABC65450.1; -; Genomic_DNA.
DR RefSeq; WP_011412614.1; NC_007716.1.
DR AlphaFoldDB; Q2NJE3; -.
DR SMR; Q2NJE3; -.
DR STRING; 322098.AYWB_333; -.
DR MEROPS; S16.001; -.
DR PRIDE; Q2NJE3; -.
DR EnsemblBacteria; ABC65450; ABC65450; AYWB_333.
DR KEGG; ayw:AYWB_333; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_14; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
DR PhylomeDB; Q2NJE3; -.
DR Proteomes; UP000001934; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0034605; P:cellular response to heat; IEA:UniProtKB-UniRule.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.130.40; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01973; lon_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027543; Lon_bac.
DR InterPro; IPR004815; Lon_bac/euk-typ.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR003111; Lon_prtase_N.
DR InterPro; IPR046336; Lon_prtase_N_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR10046; PTHR10046; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PIRSF; PIRSF001174; Lon_proteas; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00763; lon; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW Serine protease; Stress response.
FT CHAIN 1..791
FT /note="Lon protease"
FT /id="PRO_0000396534"
FT DOMAIN 28..221
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 610..791
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 697
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 740
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 374..381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 791 AA; 89748 MW; 49A885DE769EB168 CRC64;
MKTKSKKLKS DLSIGEFEDI FQEIPEQLPV VVISEIMPIP NVDFRIEVSD NSYLKALKES
ETNANSFVIL LTQKGLSHNK PKLTNLQRYG VLAQIITKVK IPHGDFKVRF RILQRVKIDK
FLQKEPFLKV SYEKVKTVYG SIEEEKALIK LVIEKIMDKP FQLLVQNTNN FLDIIKTEPE
TENITDIIIF NLKIDDLDKY KYLKESHLNK RIFYILQDIQ SLLIGLDLEQ KINEKVKQSI
DENQKEFYLR EKMKAIQLEL GDKAKKEEEI AELRDKIKKT PLPPEIKKKA LQELSRYQTS
SLMAESFVIK NYLDFLLELP WGKTSQDEND LVAIEKSLNN QHYGLQKVKE RILEYAAVKI
MTKKNPQNIL CLVGPPGVGK TSLASSIAKA LGRQFVRQSL GGLKEESEIR GHRRTYIGAM
PGRILAGIRD AKTVNPVFLL DEIDKLVTNY NFDPASALLE VLDPQQNINF MDHFLSEPFD
LSQVLFIATA NYLDNVPEAL KDRMEIIEVS SYTEKDKINI ASKYLLKKQL KNHGITDTNL
VIDNDTILYL IRHYTKEAGV RELDRILAEL ARKTVKECLI KKKEQVIITT KNVTKYLGKE
KYLNLLDEQK EKIGSTNGLA YTYFGGDLLP VEVTYYKGKG QLVLTGKLGE VLKESAYTAL
SFIKANCQNL GIDANIFAEN DFHIHLPEAA IPKDGPSAGI TIATSLVSAI TQKYIKKGLG
MTGEITLRGN ILAIGGLKEK AIAANRSGLD TIFIPQENLK DIEDIPEEVR NKLNIIPVSN
ISDVFSQVFV V
