LON_BRUAB
ID LON_BRUAB Reviewed; 812 AA.
AC P0C113; O52605; Q57D31;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=BruAb1_1112;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
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; AE017223; AAX74453.1; -; Genomic_DNA.
DR RefSeq; WP_002966840.1; NC_006932.1.
DR AlphaFoldDB; P0C113; -.
DR SMR; P0C113; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; AAX74453; AAX74453; BruAb1_1112.
DR GeneID; 3787778; -.
DR KEGG; bmb:BruAb1_1112; -.
DR HOGENOM; CLU_004109_4_3_5; -.
DR OMA; GAWQVVD; -.
DR PRO; PR:P0C113; -.
DR Proteomes; UP000000540; Chromosome I.
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..812
FT /note="Lon protease"
FT /id="PRO_0000076121"
FT DOMAIN 22..213
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 602..783
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 787..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 689
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 732
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 367..374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 812 AA; 89919 MW; DB30B60818FF6AAE CRC64;
MTGIEQKTPV GGSETGGADG LYAVLPLRDI VVFPHMIVPL FVGREKSIRA LEEVMGVDKQ
ILLATQKNAA DDDPAPDAIY EIGTIANVLQ LLKLPDGTVK VLVEGTARAK ISKFTDREDY
HEAYAAALQE PEEDAVEIEA LARSVVPDFE NYVKLNKKIS PEVVGAASQI DDYSKLADTV
ASHLAIKIPE KQEMLSVLSV RERLEKALSF MEAEISVLQV EKRIRSRVKR QMEKTQREYY
LNEQMKAIQK ELGDSEDGRD EVAEIEERIT KTKLSKEARE KALAELKKLR SMSPMSAEAT
VVRNYLDWLL SIPWGKKSKV KQDLNFAQEV LDAEHFGLGK VKERIVEYLA VQARSTKIKG
PILCLVGPPG VGKTSLARSI AKATGREYVR MSLGGVRDEA EIRGHRRTYI GSMPGKVIQS
MKKAKKSNPL FLLDEIDKMG QDFRGDPSSA MLEVLDPEQN ATFMDHYLEV EYDLSNVMFV
TTANTMNIPV PLLDRMEIIR IAGYTEDEKL EIAKRHLLPK AIKDHALQPK EFSVTEDALR
NVIRHYTREA GVRSLEREVM TLARKAVTEI LKTKKKSVKI TDKNLSDYLG VEKFRFGQID
GEDQVGVVTG LAWTEVGGEL LTIEGVMMPG KGRMTVTGNL RDVMKESISA AASYVRSRAI
DFGIEPPLFD KRDIHVHVPE GATPKDGPSA GIAMVTAIVS VLTGIPVRKD IAMTGEVTLR
GRVLPIGGLK EKLLATLRGG IKKVLIPEEN AKDLAEIPDN VKNNLEIVPV SRVGEVLKHA
LVRQPEPIEW TEQENPTAVP PVEDEAGASL AH
