(data stored in SCRATCH zone)

SWISSPROT: D7A331_STAND

ID   D7A331_STAND            Unreviewed;       813 AA.
AC   D7A331;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 68.
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   OrderedLocusNames=Snov_0416 {ECO:0000313|EMBL:ADH87749.1};
OS   Starkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 /
OS   NBRC 12443 / NCIB 9113).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Xanthobacteraceae; Starkeya.
OX   NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH87749.1, ECO:0000313|Proteomes:UP000006633};
RN   [1] {ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Beatson S., Kappler U.,
RA   Woyke T.;
RT   "Complete sequence of Starkeya novella DSM 506.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADH87749.1, ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RX   PubMed=23450099; DOI=10.4056/sigs.3006378;
RA   Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A.,
RA   Copeland A., Berry K.W., Glavina Del Rio T., Hammon N., Dalin E.,
RA   Tice H., Pitluck S., Richardson P., Bruce D., Goodwin L.A., Han C.,
RA   Tapia R., Detter J.C., Chang Y.J., Jeffries C.D., Land M., Hauser L.,
RA   Kyrpides N.C., Goker M., Ivanova N., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the facultatively chemolithoautotrophic
RT   and methylotrophic alpha Proteobacterium Starkeya novella type strain
RT   (ATCC 8093(T)).";
RL   Stand. Genomic Sci. 7:44-58(2012).
CC   -!- FUNCTION: ATP-dependent serine protease that mediates the
CC       selective degradation of mutant and abnormal proteins as well as
CC       certain short-lived regulatory proteins. Required for cellular
CC       homeostasis and for survival from DNA damage and developmental
CC       changes induced by stress. Degrades polypeptides processively to
CC       yield small peptide fragments that are 5 to 10 amino acids long.
CC       Binds to DNA in a double-stranded, site-specific manner.
CC       {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|SAAS:SAAS00004329}.
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-
CC         ProRule:PRU01122, ECO:0000256|SAAS:SAAS01117331};
CC   -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC       {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174,
CC       ECO:0000256|SAAS:SAAS00536021}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973,
CC       ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|SAAS:SAAS00004358}.
CC   -!- INDUCTION: By heat shock. {ECO:0000256|HAMAP-Rule:MF_01973}.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174,
CC       ECO:0000256|PROSITE-ProRule:PRU01122,
CC       ECO:0000256|RuleBase:RU000591, ECO:0000256|SAAS:SAAS00536024}.
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DR   EMBL; CP002026; ADH87749.1; -; Genomic_DNA.
DR   RefSeq; WP_013165254.1; NC_014217.1.
DR   STRING; 639283.Snov_0416; -.
DR   EnsemblBacteria; ADH87749; ADH87749; Snov_0416.
DR   KEGG; sno:Snov_0416; -.
DR   eggNOG; ENOG4105C6P; Bacteria.
DR   eggNOG; COG0466; LUCA.
DR   HOGENOM; HOG000261408; -.
DR   KO; K01338; -.
DR   OMA; EVIELMP; -.
DR   OrthoDB; 128102at2; -.
DR   BioCyc; SNOV639283:G1GLM-421-MONOMER; -.
DR   Proteomes; UP000006633; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; 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; 3.30.230.10; -; 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_substr-bd.
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   2: Evidence at transcript level;
DR   PRODOM; D7A331.
DR   SWISS-2DPAGE; D7A331.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01973,
KW   ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PIRSR:PIRSR001174-2,
KW   ECO:0000256|RuleBase:RU000591}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006633};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973,
KW   ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|SAAS:SAAS00417288};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01973,
KW   ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122,
KW   ECO:0000256|RuleBase:RU000591};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01973,
KW   ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PIRSR:PIRSR001174-2,
KW   ECO:0000256|RuleBase:RU000591};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_01973,
KW   ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122,
KW   ECO:0000256|RuleBase:RU000591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006633};
KW   Serine protease {ECO:0000256|HAMAP-Rule:MF_01973,
KW   ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122,
KW   ECO:0000256|RuleBase:RU000591};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_01973,
KW   ECO:0000256|SAAS:SAAS00070204}.
FT   DOMAIN       36    227       Lon N-terminal. {ECO:0000259|PROSITE:
FT                                PS51787}.
FT   DOMAIN      617    798       Lon proteolytic. {ECO:0000259|PROSITE:
FT                                PS51786}.
FT   NP_BIND     381    388       ATP. {ECO:0000256|HAMAP-Rule:MF_01973,
FT                                ECO:0000256|PIRSR:PIRSR001174-2}.
FT   COILED      142    162       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    704    704       {ECO:0000256|HAMAP-Rule:MF_01973,
FT                                ECO:0000256|PIRSR:PIRSR001174-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   ACT_SITE    747    747       {ECO:0000256|HAMAP-Rule:MF_01973,
FT                                ECO:0000256|PIRSR:PIRSR001174-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU01122}.
SQ   SEQUENCE   813 AA;  88718 MW;  522FA590B7C91BDC CRC64;
     MTHPDFERFD PVRMADAGGN NGASGATNGN VPADQLIVLP VRNFVLFPGV VLPLSVGRAA
     SIAAAQQAVR EGRPIGILMQ RDASVEEPSP TDLHRMGVVA NILRYVTAPD GTHHLVLQGE
     QRFHVDEFVR EKPFVTARVK RLEESEERSS EIEARFVHLQ GQATEALELL PQVPAELVAA
     VRGSNSPAGL ADLVAAYIDI SADEKQELLE TVDIVARMNK VSRLLAHRIE VLRLSQEISK
     QTKASLDERQ REVLLREQMA AIQKQLGEDD GNSQDIADLE KAITDAGMPE DVEQMARKEL
     GRLRRMQDAS AEYGMVRTYL DWLIALPWKL PETAPIDIAE ARKILDEDHF GLDKIKRRIV
     EYLAVRKLAP GGKAPILCFA GPPGVGKTSL GQSIARAMGR KFVRVSLGGV HDEAEIRGHR
     RTYVGALPGN IIQGIRKAGT RDCVMMLDEI DKMGSGIQGD PSAAMLEVLD PEQNGTFRDN
     YLGVPFDLSR VVFIATANML DTIPGPLRDR MEIIQLTGYT DTEKLQIAKR YLVRRQLEAN
     GVKPEQVEVD DEALKAIIRA YTREAGVRNL EREVGRAVRH VAVGIAEGSV SHARISVDTL
     PEMLGPPIFE DEVALRVSVP GVATGLAWTP VGGDILFIEA TRVPGRGGLI LTGQLGDVMK
     ESAQAAWSLV KSRAEELGID PELFAKNDVH VHVPAGATPK DGPSAGVAMF TALVSLLTGR
     TVRKDTAMTG EISLRGLVLP VGGIKEKVVA AARAGLTRVM LPARNRRDYE DIPQDARDRL
     EFVWLERVDE AMANALEPRE SPDQPALPLK AAS
//

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