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Database: UniProt
Entry: W8VWJ1_9FLAO
LinkDB: W8VWJ1_9FLAO
Original site: W8VWJ1_9FLAO 
ID   W8VWJ1_9FLAO            Unreviewed;       816 AA.
AC   W8VWJ1;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 57.
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=NMS_2379 {ECO:0000313|EMBL:BAO56388.1};
OS   Nonlabens marinus S1-08.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Nonlabens.
OX   NCBI_TaxID=1454201 {ECO:0000313|EMBL:BAO56388.1, ECO:0000313|Proteomes:UP000031760};
RN   [1] {ECO:0000313|EMBL:BAO56388.1, ECO:0000313|Proteomes:UP000031760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S1-08 {ECO:0000313|EMBL:BAO56388.1,
RC   ECO:0000313|Proteomes:UP000031760};
RX   PubMed=24706784; DOI=10.1073/pnas.1403051111;
RA   Yoshizawa S., Kumagai Y., Kim H., Ogura Y., Hayashi T., Iwasaki W.,
RA   DeLong E.F., Kogure K.;
RT   "Functional characterization of flavobacteria rhodopsins reveals a unique
RT   class of light-driven chloride pump in bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:6732-6737(2014).
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}.
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DR   EMBL; AP014548; BAO56388.1; -; Genomic_DNA.
DR   RefSeq; WP_041496877.1; NZ_AP014548.1.
DR   AlphaFoldDB; W8VWJ1; -.
DR   STRING; 1454201.NMS_2379; -.
DR   HOGENOM; CLU_004109_4_3_10; -.
DR   OrthoDB; 9803599at2; -.
DR   Proteomes; UP000031760; 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   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:SF64; 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|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01973};
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          44..237
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51787"
FT   DOMAIN          626..807
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   ACT_SITE        713
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT                   ECO:0000256|PIRSR:PIRSR001174-1"
FT   ACT_SITE        756
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT                   ECO:0000256|PIRSR:PIRSR001174-1"
FT   BINDING         391..398
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   816 AA;  92267 MW;  4CE349E590B5F79B CRC64;
     MFKPKKFQID IMSQQEFDQD AEFIPLLSSK DEEEMNAEAV PETLAILPLR NMVLFPGVVI
     PITAGRDQSI KLLQEANKNN EAIGVVAQKD ESVEDPGQED LHTTGVVARI LKVFKMPDGN
     TTVIIQGKKR FEIDNIVETE PYLKATTKSV VEARPAAENE EFNAIIEKIK ELSLEIIKES
     PNIPSEASFA IKNIESNSFL VNFVSSNMNL KVEDKQNLLE INDLKDRALE TLKFMNVERQ
     KLELKNDIQS RVQTDINKQQ REYFLHQQMK TIQEELGGGV SSHQEIDEMR QRAKTKKWDD
     KVKEHFEKEL AKMQRMNPQV AEFSIQRNYL DLILDLPWNE YSKDNFDLKR AMKILDRDHY
     GLDDVKKRII EYLAVLKLRN DMKSPILCLY GPPGVGKTSL GKSIAEALGR EYVRISLGGL
     RDEAEIRGHR KTYIGAMPGR IIQSIKKAKT SNPVFVLDEI DKLSSSNNGD PSSAMLEVLD
     PEQNNSFYDN FLEMGFDLSK VMFVATSNSL QTIQPALRDR MEIINVTGYT IEEKVEIGKR
     HLLPKQLKEH GMQKDQFKLA KPQIEKIVEG YTRESGVRSL DKQIAKMVRY AAKSIAMEDP
     YDLKVTNETV IEVLGAPRMR DKYENNDVAG VVTGLAWTRV GGDILFIESI LSKGKGQLNI
     TGNLGKVMKE SATIAMEYIK AHAEELGINP ETFDKYNVHI HVPEGATPKD GPSAGITMLT
     SLVSLFTQRK VKKSIAMTGE ITLRGKVLPV GGIKEKILAA KRARIKEILL CEQNRRDIEE
     IKADYLKGLT FHYVSDMSNV LELALTKQKV KNAKVL
//
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