(data stored in SCRATCH zone)

SWISSPROT: D1CEU8_THET1

ID   D1CEU8_THET1            Unreviewed;       808 AA.
AC   D1CEU8;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 77.
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=Tter_0536 {ECO:0000313|EMBL:ACZ41454.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41454.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41454.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
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; CP001825; ACZ41454.1; -; Genomic_DNA.
DR   STRING; 525904.Tter_0536; -.
DR   EnsemblBacteria; ACZ41454; ACZ41454; Tter_0536.
DR   KEGG; ttr:Tter_0536; -.
DR   eggNOG; ENOG4105C6P; Bacteria.
DR   eggNOG; COG0466; LUCA.
DR   HOGENOM; HOG000261408; -.
DR   KO; K01338; -.
DR   OMA; EVIELMP; -.
DR   BioCyc; TTER525904:G1GGS-542-MONOMER; -.
DR   Proteomes; UP000000323; Chromosome 1.
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; D1CEU8.
DR   SWISS-2DPAGE; D1CEU8.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01973,
KW   ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PIRSR:PIRSR001174-2,
KW   ECO:0000256|RuleBase:RU000591};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
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:UP000000323};
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       15    206       Lon N-terminal. {ECO:0000259|PROSITE:
FT                                PS51787}.
FT   DOMAIN      619    801       Lon proteolytic. {ECO:0000259|PROSITE:
FT                                PS51786}.
FT   NP_BIND     383    390       ATP. {ECO:0000256|HAMAP-Rule:MF_01973,
FT                                ECO:0000256|PIRSR:PIRSR001174-2}.
FT   ACT_SITE    707    707       {ECO:0000256|HAMAP-Rule:MF_01973,
FT                                ECO:0000256|PIRSR:PIRSR001174-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   ACT_SITE    750    750       {ECO:0000256|HAMAP-Rule:MF_01973,
FT                                ECO:0000256|PIRSR:PIRSR001174-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU01122}.
SQ   SEQUENCE   808 AA;  90313 MW;  2B84426D0CD1BECF CRC64;
     MNNQEQPEAN IPSLLPVLPL RDSVIYPFAV LPIVVGQERS IRLVDDSMRS RRLIVLVAQR
     SRNVEQAGPD DIYRIGTVAT IHHLVRAPDG TLRIVVQGVQ RVRILDFIST QPYLVARIDP
     APDQTENNVE EEALRRVAVD LFRRMVEISP DLPNEILPTL DSIQDPIQTF YFIAGAIQLD
     VDTRQELLEL EPLEVKLRRL VEILQKELSI REISQRIQSE TQERLTQAQR EAYLREQLRT
     IQSQLGEGPE QSEVNELRRR IEEAGLPEEA RKEAERELNR LSTIPMASPE YAIIRTYLEW
     LADLPWNKLS GGTIDTQRAR EILDEDHYDL EKVKDRIIEH LAVRKLREQR VSNLSGQEGT
     GEQNTIPSGS GDTLREPILC FVGPPGVGKT SLGQSIARAL GRKFIRMSLG GIRDEAEIRG
     HRRTYIGAMP GRIIQGMRRV GTKDPVFMLD EIDKITVGFQ GDPAAALLEV LDPAQNHSFV
     DNYLGVPFDL SQVLFIATAN TLDTIPAPLL DRMEVIQISG YTEQEKLFIA QRYLIPKQMR
     AHGIQDSELR FTEESIRKII REYTQEAGVR NLDRQIATIC RKVARAIADG AAQSIEITPD
     NLQEYLGHPR HFHSTAERIT RPGVATGLAW TPTGGEILFI EATMMPDPHP RVILTGMLGE
     VMRESAQIAL SYVRSEADPL GVNPDAFTGK TVHIHVPAGA IPKDGPSAGL AIVAALASLG
     SSRLVRSDVA MTGEITLRGK VLPVGGIKEK VLAAHRAGIK TVILPKENEQ DLEDIPQELR
     DQMRFVLVDN IEDAMQVALT ELPVLEET
//

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