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Database: UniProt
Entry: A0A139SVS1_9GAMM
LinkDB: A0A139SVS1_9GAMM
Original site: A0A139SVS1_9GAMM 
ID   A0A139SVS1_9GAMM        Unreviewed;       800 AA.
AC   A0A139SVS1;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=AXE65_00055 {ECO:0000313|EMBL:KXU38594.1};
OS   Ventosimonas gracilis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Ventosimonadaceae; Ventosimonas.
OX   NCBI_TaxID=1680762 {ECO:0000313|EMBL:KXU38594.1, ECO:0000313|Proteomes:UP000072660};
RN   [1] {ECO:0000313|EMBL:KXU38594.1, ECO:0000313|Proteomes:UP000072660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CV58 {ECO:0000313|EMBL:KXU38594.1,
RC   ECO:0000313|Proteomes:UP000072660};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) 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}.
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:KXU38594.1}.
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DR   EMBL; LSZO01000112; KXU38594.1; -; Genomic_DNA.
DR   RefSeq; WP_068388921.1; NZ_LSZO01000112.1.
DR   AlphaFoldDB; A0A139SVS1; -.
DR   OrthoDB; 9803599at2; -.
DR   Proteomes; UP000072660; 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   DNA-binding {ECO:0000313|EMBL:KXU38594.1};
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:UP000072660};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW   Rule:MF_01973}; Stress response {ECO:0000256|HAMAP-Rule:MF_01973}.
FT   DOMAIN          6..198
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51787"
FT   DOMAIN          587..768
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   REGION          773..800
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        674
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT                   ECO:0000256|PIRSR:PIRSR001174-1"
FT   ACT_SITE        717
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT                   ECO:0000256|PIRSR:PIRSR001174-1"
FT   BINDING         352..359
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   800 AA;  89083 MW;  5F1C3C64BD7E9DFC CRC64;
     MKTKVLPFLP LRDVVVYPQM VIPLFIGRDK SVQALDEAMS CDKQILLLTQ HSPSDDEPSE
     ATLYRVGTVA TILQMLKLQN GTLKVLVEGG QRAEVLHFAD LASDYQAEVA LLDEQELEEP
     TAQEAFVRSL RRQFEQYAEQ GRKVPREILA SLHAIDEPGR LIDAMAAHMP LKIEQKQKVL
     EINDIAERAR HFLGLLEAEI ELLQVEQHIR GHVKKQMERN HREYYLNEQM KAIQKELGSG
     EDGHNEVDAL QKRIEQAALS QEAKKRAETE LRKLRQMPPM SAETTVVRTY LDWLVGLPWQ
     AQSRVRHDLP RAEAILEAEH YGLKEVKERI LEYLAVQKRV KIAKGPVLCL VGPPGVGKTS
     LAESIARATN RKFVRMALGG VRDEAEIRGH RRTYIGSMPG RLLQKMSKAG VRNPLFLLDE
     IDKMGQDMRG DPASALLEVL DPEQNHSFND HYLEVDYDLS GVMFLCTANS MNIPPALLDR
     MEIIRLPGYT EDEKQNIALK YLLPKQLKES GLKKSELALA PEAVLAIIRH YTREAGVRSL
     ERQLAKLCRK VVRKYAGEKQ LKLTLSAADL EPLLGVRKYR FGLAEQDNQI GQVNGLAWTE
     VGGELLRIEA AAVAGKGQLI KTGSLGDVMG ESITAALTVV RSRAQSLGLA ADFQEKNDIH
     IHVPEGATPK DGPSAGIGMC TALVSVLTQI PVRADVAMTG EITLRGQVLA IGGLKEKLLA
     AHRGGIKTVI IPEENQRDLK EIPENIQQNL QIKAVKWIDE VLQIALQYAP QPLPCTTANP
     TGKKPRQKDD AQGGRQISTH
//
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