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Lon protease (EC 3.4.21.53) (ATP-dependent protease La)

 A9I3N6_BORPD            Unreviewed;       782 AA.
A9I3N6;
05-FEB-2008, integrated into UniProtKB/TrEMBL.
05-FEB-2008, sequence version 1.
22-NOV-2017, entry version 84.
RecName: Full=Lon protease {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
EC=3.4.21.53 {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
AltName: Full=ATP-dependent protease La {ECO:0000256|HAMAP-Rule:MF_01973};
Name=Ion2 {ECO:0000313|EMBL:CAP44197.1};
Synonyms=lon {ECO:0000256|HAMAP-Rule:MF_01973};
OrderedLocusNames=Bpet3852 {ECO:0000313|EMBL:CAP44197.1};
Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Alcaligenaceae; Bordetella.
NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP44197.1, ECO:0000313|Proteomes:UP000001225};
[1] {ECO:0000313|EMBL:CAP44197.1, ECO:0000313|Proteomes:UP000001225}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
{ECO:0000313|Proteomes:UP000001225};
PubMed=18826580; DOI=10.1186/1471-2164-9-449;
Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A.,
Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J.,
Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N.,
Larisch C., Link S., Linke B., Meyer F., Mormann S., Nakunst D.,
Rueckert C., Schneiker-Bekel S., Schulze K., Vorhoelter F.J.,
Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B.,
Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R.;
"The missing link: Bordetella petrii is endowed with both the
metabolic versatility of environmental bacteria and virulence traits
of pathogenic Bordetellae.";
BMC Genomics 9:449-449(2008).
-!- FUNCTION: ATP-dependent serine protease that mediates the
selective degradation of mutant and abnormal proteins as well as
certain short-lived regulatory proteins. Required for cellular
homeostasis and for survival from DNA damage and developmental
changes induced by stress. Degrades polypeptides processively to
yield small peptide fragments that are 5 to 10 amino acids long.
Binds to DNA in a double-stranded, site-specific manner.
{ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|SAAS:SAAS00004329}.
-!- CATALYTIC ACTIVITY: Hydrolysis of proteins in presence of ATP.
{ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174,
ECO:0000256|SAAS:SAAS00338825}.
-!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
{ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174,
ECO:0000256|SAAS:SAAS00536021}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973,
ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|SAAS:SAAS00007367}.
-!- INDUCTION: By heat shock. {ECO:0000256|HAMAP-Rule:MF_01973}.
-!- SIMILARITY: Belongs to the peptidase S16 family.
{ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174,
ECO:0000256|PROSITE-ProRule:PRU01122,
ECO:0000256|RuleBase:RU000591, ECO:0000256|SAAS:SAAS00536024}.
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EMBL; AM902716; CAP44197.1; -; Genomic_DNA.
ProteinModelPortal; A9I3N6; -.
STRING; 340100.Bpet3852; -.
EnsemblBacteria; CAP44197; CAP44197; Bpet3852.
KEGG; bpt:Bpet3852; -.
eggNOG; ENOG4105C6P; Bacteria.
eggNOG; COG0466; LUCA.
HOGENOM; HOG000261408; -.
KO; K01338; -.
OMA; ADMPGNG; -.
OrthoDB; POG091H00WA; -.
Proteomes; UP000001225; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
GO; GO:0033554; P:cellular response to stress; IEA:UniProtKB-UniRule.
GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
Gene3D; 3.30.230.10; -; 1.
HAMAP; MF_01973; lon_bact; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR027543; Lon_bac.
InterPro; IPR004815; Lon_bac/euk-typ.
InterPro; IPR008269; Lon_proteolytic.
InterPro; IPR027065; Lon_Prtase.
InterPro; IPR003111; Lon_substr-bd.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008268; Peptidase_S16_AS.
InterPro; IPR015947; PUA-like_sf.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
PANTHER; PTHR10046; PTHR10046; 1.
Pfam; PF00004; AAA; 1.
Pfam; PF05362; Lon_C; 1.
Pfam; PF02190; LON_substr_bdg; 1.
PIRSF; PIRSF001174; Lon_proteas; 1.
SMART; SM00382; AAA; 1.
SMART; SM00464; LON; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF88697; SSF88697; 1.
TIGRFAMs; TIGR00763; lon; 1.
PROSITE; PS51787; LON_N; 1.
PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PROSITE; PS01046; LON_SER; 1.
2: Evidence at transcript level;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01973,
ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PIRSR:PIRSR001174-2,
ECO:0000256|RuleBase:RU000591};
Complete proteome {ECO:0000313|Proteomes:UP000001225};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973,
ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|SAAS:SAAS00004285};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_01973,
ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122,
ECO:0000256|RuleBase:RU000591};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01973,
ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PIRSR:PIRSR001174-2,
ECO:0000256|RuleBase:RU000591};
Protease {ECO:0000256|HAMAP-Rule:MF_01973,
ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122,
ECO:0000256|RuleBase:RU000591};
Reference proteome {ECO:0000313|Proteomes:UP000001225};
Serine protease {ECO:0000256|HAMAP-Rule:MF_01973,
ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122,
ECO:0000256|RuleBase:RU000591};
Stress response {ECO:0000256|HAMAP-Rule:MF_01973,
ECO:0000256|SAAS:SAAS00004281}.
DOMAIN 12 203 Lon N-terminal.
{ECO:0000259|PROSITE:PS51787}.
DOMAIN 594 769 Lon proteolytic.
{ECO:0000259|PROSITE:PS51786}.
NP_BIND 357 364 ATP. {ECO:0000256|HAMAP-Rule:MF_01973,
ECO:0000256|PIRSR:PIRSR001174-2}.
ACT_SITE 675 675 {ECO:0000256|HAMAP-Rule:MF_01973,
ECO:0000256|PIRSR:PIRSR001174-1,
ECO:0000256|PROSITE-ProRule:PRU01122}.
ACT_SITE 718 718 {ECO:0000256|HAMAP-Rule:MF_01973,
ECO:0000256|PIRSR:PIRSR001174-1,
ECO:0000256|PROSITE-ProRule:PRU01122}.
SEQUENCE 782 AA; 85348 MW; 69D92B4D5A5FCC09 CRC64;
MSDTRTLPDD ARIIIPLRDA VLFPGVLSPV TVRRASSVAA AQEAVKNEHP VGFLLQRDPS
KDEIGPDDLR WVGTEGPIAR YITGQDGAHH LLVQGQSRFR VLEFLDGWPF MVARVAEIPA
AEDHDSQTEA RFLQLKEQAI DAITLLPNVP DELIGVVRGI ESAGLLADMV THMIDIKPEQ
KQDILETFDL SRRLDQVIEL LAGRVEVLRL SKEIGDRTRA QFDERQRETV LREQLRQIQK
ELGDVDDSAA EVARLKDAIE AAGMPDEVLS HARKELGRLQ RMGETSGESA MLRTYLEWLT
ELPWKQQPQP PIDLAEARKV LDEDHFGLDK IKRRILEYLA VRKLNPQGRS PILCFAGPPG
VGKTSLGQSI ARATGRVFQR VALGGVHDEA EIRGHRRTYL GALPGNIIQA MRRAGTNNAV
VMLDEIDKLG AGGFHGDPGS ALLEVLDPEQ NHKFRDNYLG VDFDLSHVMF ICTANMLETI
PGPLRDRMEI IQLPGYTEEE KVQIARRYLV RRQLEANGLT AGQAELSDAA LSSIVGDYTR
EAGVRQLERE IGAVLRHAAM QIAEGKATHV AIDAPDLPAI LGAHRFENEV ALRTGVPGVA
TGLAWTPVGG DILFIEASKT PGSGRLILTG QLGDVMKESA QAALTLAKIW SGDSLEKTDV
HIHVPAGATP KDGPSAGVAM FLALASLLSG RPVRSDVAMT GEISLRGLVL PIGGVKEKTL
AALRAGITTV MIPRRNEKDL DDVPAEARAK LKFLLLDRIE DAIRYAIDGQ EAPVAEPVAQ
AG


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