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Database: UniProt
Entry: A0A2N5I4L4_9BACI
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Original site: A0A2N5I4L4_9BACI 
ID   A0A2N5I4L4_9BACI        Unreviewed;       775 AA.
AC   A0A2N5I4L4;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
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   ECO:0000313|EMBL:PLS16891.1};
GN   ORFNames=CVD28_14650 {ECO:0000313|EMBL:PLS16891.1};
OS   Bacillus sp. M6-12.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2054166 {ECO:0000313|EMBL:PLS16891.1, ECO:0000313|Proteomes:UP000234907};
RN   [1] {ECO:0000313|EMBL:PLS16891.1, ECO:0000313|Proteomes:UP000234907}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M6-12 {ECO:0000313|EMBL:PLS16891.1,
RC   ECO:0000313|Proteomes:UP000234907};
RA   Seuylemezian A., Cooper K., Vaishampayan P.;
RT   "Comparitive Functional Genomics of Dry Heat Resistant strains isolated
RT   from the Viking Spacecraft.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|RuleBase:RU000591}.
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:PLS16891.1}.
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DR   EMBL; PGVF01000013; PLS16891.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N5I4L4; -.
DR   OrthoDB; 9803599at2; -.
DR   Proteomes; UP000234907; 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; IPR008268; Peptidase_S16_AS.
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.
DR   PROSITE; PS01046; LON_SER; 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   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW   Rule:MF_01973}; Stress response {ECO:0000256|HAMAP-Rule:MF_01973}.
FT   DOMAIN          9..200
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51787"
FT   DOMAIN          590..771
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   ACT_SITE        677
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT                   ECO:0000256|PIRSR:PIRSR001174-1"
FT   ACT_SITE        720
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT                   ECO:0000256|PIRSR:PIRSR001174-1"
FT   BINDING         354..361
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   775 AA;  86932 MW;  F6926C879C6AB2C8 CRC64;
     MADRKEFIVP LLPLRGLLVY PTMVLHLDVG REKSVQALEK AMVEDHLIFL TTQKDVSLDE
     PGEDDIYKMG TLTKVKQMLK LPNGTIRVLV EGLNRAEIIS VTDHETYFSA KVEVYEDSEE
     KEIEHQALMR TLLEYFEQYI KMSKKISAET FSATSDIEEP GRLADIIASH LPLKQKEKQE
     ILETIDVRKR LSRVIEIINN EREVLNLEKK IGQRVKRSME RTQKEYYLRE QMKAIQKELG
     DKEGKTGEIA DLTEKIEKAG MPENIEATAF RELDRYEKVP ASSAESAVIR NYIEWLVSLP
     WSNATKDDLN IHKAEKILNS EHFGLEKVKE RVLEYLAVQQ LTNSLKGPIL CLAGPPGVGK
     TSLAKSIATS MNRNFVRISL GGVRDESEIR GHRRTYVGAM PGRIIQGMRK AGTINPVFLL
     DEVDKMSSDF RGDPSSAMLE VLDPEQNHNF SDHYIEETYD LSKVMFIATA NNLATIPGPL
     RDRMEIITIS GYTEIEKLHI AKDHLLPRQL KDHGLKKAQL QIRDDAMLRI IRYYTREAGV
     RSLERQLASI CRKTAKIIVS EEKKRVVISD GGVEDFLGKT MYHYGQAELE DQVGVATGLA
     YTTVGGDTLQ IEVSLSPGKG KLVLTGKLGD VMKESAQAAF SYVRSKAAEL NIETDFNEKY
     DIHIHVPEGA VPKDGPSAGI TMATALISAL TGRPIRREVG MTGEITLRGR VLPIGGLKEK
     SLSAHRAGLT KIICPKDNEK DIDDIPESVR NELEFVLVSH VDEVIQHALL AGESK
//
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