ID A0A063XZQ0_9GAMM Unreviewed; 814 AA.
AC A0A063XZQ0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Lon protease {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
DE EC=3.4.21.53 {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
DE AltName: Full=ATP-dependent protease La {ECO:0000256|HAMAP-Rule:MF_01973};
GN Name=lon {ECO:0000256|HAMAP-Rule:MF_01973};
GN ORFNames=ADINL_2865 {ECO:0000313|EMBL:KDE38410.1};
OS Nitrincola lacisaponensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Nitrincola.
OX NCBI_TaxID=267850 {ECO:0000313|EMBL:KDE38410.1, ECO:0000313|Proteomes:UP000027318};
RN [1] {ECO:0000313|EMBL:KDE38410.1, ECO:0000313|Proteomes:UP000027318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4CA {ECO:0000313|EMBL:KDE38410.1,
RC ECO:0000313|Proteomes:UP000027318};
RX PubMed=16280482; DOI=10.1099/ijs.0.63647-0;
RA Dimitriu P.A., Shukla S.K., Conradt J., Marquez M.C., Ventosa A.,
RA Maglia A., Peyton B.M., Pinkart H.C., Mormile M.R.;
RT "Nitrincola lacisaponensis gen. nov., sp. nov., a novel alkaliphilic
RT bacterium isolated from an alkaline, saline lake.";
RL Int. J. Syst. Evol. Microbiol. 55:2273-2278(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:0000256|HAMAP-Rule:MF_01973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01973,
CC ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122};
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}.
CC -!- INDUCTION: By heat shock. {ECO:0000256|HAMAP-Rule:MF_01973}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP-
CC Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
CC ProRule:PRU01122}.
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:KDE38410.1}.
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DR EMBL; JMSZ01000042; KDE38410.1; -; Genomic_DNA.
DR RefSeq; WP_051632857.1; NZ_JMSZ01000042.1.
DR AlphaFoldDB; A0A063XZQ0; -.
DR STRING; 267850.ADINL_2865; -.
DR PATRIC; fig|267850.7.peg.2816; -.
DR OrthoDB; 9803599at2; -.
DR Proteomes; UP000027318; Unassembled WGS sequence.
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 CDD; cd19500; RecA-like_Lon; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.5.5270; -; 1.
DR Gene3D; 1.20.58.1480; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 2.30.130.40; LON domain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00763; lon; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF56; LON PROTEASE; 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 PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01973};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01973,
KW ECO:0000256|PIRNR:PIRNR001174};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01973};
KW Reference proteome {ECO:0000313|Proteomes:UP000027318};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_01973};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_01973}.
FT DOMAIN 20..211
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 603..784
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 690
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT ACT_SITE 733
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT BINDING 366..373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 814 AA; 90798 MW; B9B0EFFBEE8C14AA CRC64;
MDHFEAIEDN AGRGRVDIEL PVLPLRDVVV YPHMVIPLFV GRAKSIRALD NALAHNKQIV
LVAQKSASED EPAASDLFHV GTVATILQML KLPDGTVKVL VEGEYRARIA CLTDHEDCFS
ASLEVMVTEE ATEAESEIYK HTALDQFERF IQINKKIPSE VLSSLQNIDD IGRLADTLAA
HMALKLDEKQ KVLEMLGSRE RLEYLMAKME TEIDLVEVEK RIRGRVKKQM EKSQREYYLN
EQMKAIQKEL GDMDETGGND MDELRRRIEA AGMPEEALKK TLAEHKKLQM MSPMSAEATV
VRGYIDWMLQ VPWTKRSKVR LDMQRAQNIL DEDHFGLEEV KERIIEYLAV QKRVRKLKGP
ILCLVGPPGV GKTSLGKSIA RATNREYVRM ALGGVRDEAE IRGHRRTYIG SMPGKLVQKI
TKAGVKNPLF LLDEIDKMGM DHRGDPSSAL LEVLDPEQNS TFNDHYLEVD MDLSDVLFIC
TSNSMNIPGP LLDRMEIIRI PGYTEDEKLN IAKKYLIPKQ MKQSGLKSGE LVFTDEAILD
LIRYYTREAG VRGLEREIAK ICRKAVREFA LGKMTEALQQ VTAENLEHYS GVHKHNYGKA
EEEDLVGHVT GLAWTQVGGE ILSIEAAIVP GKGRQIHTGS LGDVMKESIQ AALTVVRNRS
VQLGIRPDFH EKQDIHIHVP EGATPKDGPS AGIGMCTALI SALTGIPVRS DVAMTGEITL
RGQVLPIGGL KEKLLAAHRG GIKTVVIPDE NKRDLKEIPE NIKADLDIIA VKWIDEVLEV
ALTRSPEPLD EKEAEIVAKE SAGVKPEPGQ LSTH
//
