LON_WOLPP
ID LON_WOLPP Reviewed; 818 AA.
AC B3CLB3;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=WP0572;
OS Wolbachia pipientis subsp. Culex pipiens (strain wPip).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=570417;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=wPip;
RX PubMed=18550617; DOI=10.1093/molbev/msn133;
RA Klasson L., Walker T., Sebaihia M., Sanders M.J., Quail M.A., Lord A.,
RA Sanders S., Earl J., O'Neill S.L., Thomson N., Sinkins S.P., Parkhill J.;
RT "Genome evolution of Wolbachia strain wPip from the Culex pipiens group.";
RL Mol. Biol. Evol. 25:1877-1887(2008).
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; AM999887; CAQ54680.1; -; Genomic_DNA.
DR RefSeq; WP_007302001.1; NC_010981.1.
DR AlphaFoldDB; B3CLB3; -.
DR SMR; B3CLB3; -.
DR STRING; 570417.WP0572; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; CAQ54680; CAQ54680; WP0572.
DR KEGG; wpi:WP0572; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_5; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000008814; 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; 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.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW Serine protease; Stress response.
FT CHAIN 1..818
FT /note="Lon protease"
FT /id="PRO_0000396616"
FT DOMAIN 14..214
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 605..786
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 692
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 735
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 370..377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 818 AA; 91809 MW; DFC5DFEC4A66F355 CRC64;
MSIGRAVNFN STVLPVLPLR DVVIFPNIML PLFVGREKSV HALEYAISSS SHQNEIFLIA
QKDGSIDNPE PENLYEVGVL ANIIQPLIKL PDNAVKVMIH GVRRGRVIEY ISSHTLLQAR
VALDGHYEYG ENEDNIDLEA LRRSVIDAFD NWCKLSKKSR PEIIIDPIDQ VKEVNQIVDM
IASHLNIKVS DKQNILEVYN PKERLKKVFA LIEREISILS AQNRLYKTIK SQVESTQKVY
YLNEQLKAIQ KELGEFENGD EGNILNEFEK KINETKLSEE AKEKAITDLK RYKKMNPISP
EATVISSYLH WLLDLPWGKY KDAKINLNAA KKILDENHYG IEKVKDRIIE FLAVLKRVKE
IKGPILCLVG PPGVGKTSLA KSMAKAVGRD FVRISLGGIR DESEIRGHRK TYIGSMPGKI
IQHMKKANSC NPLFLLDEID KMGSDSRGDP ASALLEVLDT EHNKHFTDHY LEVEFDLSSV
MFVATANSLN LPHPLRDRME IIQLSGYTED EKISIATHHL IPKLKKEHGL HQKEWEITNE
ALYELIRLYT RESGVRSMER ELAKLMRKAV KAILTDKNKK ISVETGNLQD YLGVRKYTFG
IAENESLVGI VTGLAYTETG GDILMIESVL IPGKGEIKYT GKLGEVMQES IKAAYSYVRS
NCLFFGIKPE KFQNNDIHLH VPEGAVPKDG PSAGSAVCTS IVSLMTNIPV NKSVAMTGEV
TLRGRVLAIG GLREKLLAAL RGSIKTVIIP SENEKDMQEI PANIKEEINV IFAENIDEVI
KVALMHPITS IDDNNEISVS TSIENKDNTF PSSETLKH
