LON2_SORC5
ID LON2_SORC5 Reviewed; 804 AA.
AC A9GBF1;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Lon protease 2 {ECO:0000255|HAMAP-Rule:MF_01973};
DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_01973};
DE AltName: Full=ATP-dependent protease La 2 {ECO:0000255|HAMAP-Rule:MF_01973};
GN Name=lon2 {ECO:0000255|HAMAP-Rule:MF_01973}; OrderedLocusNames=sce2838;
OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS ce56)).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; Sorangiineae;
OC Polyangiaceae; Sorangium.
OX NCBI_TaxID=448385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce56;
RX PubMed=17965706; DOI=10.1038/nbt1354;
RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA Puehler A., Mueller R.;
RT "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL Nat. Biotechnol. 25:1281-1289(2007).
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:0000255|HAMAP-Rule:MF_01973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01973};
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- INDUCTION: By heat shock. {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_01973}.
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DR EMBL; AM746676; CAN92997.1; -; Genomic_DNA.
DR RefSeq; WP_012235470.1; NC_010162.1.
DR AlphaFoldDB; A9GBF1; -.
DR SMR; A9GBF1; -.
DR STRING; 448385.sce2838; -.
DR EnsemblBacteria; CAN92997; CAN92997; sce2838.
DR KEGG; scl:sce2838; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_7; -.
DR OrthoDB; 128102at2; -.
DR BioCyc; SCEL448385:SCE_RS14560-MON; -.
DR Proteomes; UP000002139; 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 Gene3D; 2.30.130.40; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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_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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW Reference proteome; Serine protease; Stress response.
FT CHAIN 1..804
FT /note="Lon protease 2"
FT /id="PRO_0000396601"
FT DOMAIN 19..214
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 603..784
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 782..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 690
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 733
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 367..374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 804 AA; 88646 MW; 967DCBD04474DE28 CRC64;
MPTGDPSSRT PPSPDADSVP ILPLRNSVLF PMSVVPINVG RPRSVRLVED LLGRERALVG
VISQRSPDVD EPTFKELYSV GTVARVVKVI RLGPNNYSVV LNGLGRFRVK SAFSLEPYMR
ARIERIPESL VRDVELEALG AGLREATREV LGLMPNLPRD TAGILDNVRE PGALADLIAS
NFPQAQASVG DKQEILEAFD VKARVRLVLA MVGRQLEVLR VKKEISSMVQ EEMGKSQREY
ILRQQMKSIK EELGEGGDDD EIEELRERIR RAKVPAEVDK VVRKQLSRLR SMAQQSAEFN
VTKTYLEWIA DLPWSKTTVD KLSVESVRRC LDEDHLGLEK VKKRIVEYSA IRQLRTDKKG
PILLFIGPPG VGKTSLGKSI ARSMGRRYER IALGGVRDEA EIRGHRRTYV GALPGRILQA
LKKAGTKNPV LVLDEVDKMG VDLRGDPAAA LLEVLDPEQN STFQDHYLDL PFDLSQVMFL
ATANNWDGIP GPLVDRMEVI EVPGYTRTDK LGIAREFLVP KQLSAHGLTD ERLEFTEPGI
EAVVDHYTRE AGVRGLERQI AAVCRATAVK VAEGNDVREV ATPEHVEQVL GPHKHRPEIA
ERTLQPGVAT GLAWTPAGGE ILFIEATKMP GKGNVVLTGN MRNVMQESAS TAVSFVRSKA
DRLHLDPEWL KEIDLHVHIP QHGTPKDGPS AGVTMFAAVA SLLLGAPVRS DVAMTGEISL
RGRVMPVGGV KEKLLAAHRA GIRHVLIPAK NRRDLEDVPQ DVKDQIKITM VSSMEEILPL
VLEPPRRAPA QSASPEELEE QAGV
