LON4_SORC5
ID LON4_SORC5 Reviewed; 799 AA.
AC A9F8L0;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Lon protease 4 {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 4 {ECO:0000255|HAMAP-Rule:MF_01973};
GN Name=lon4 {ECO:0000255|HAMAP-Rule:MF_01973}; OrderedLocusNames=sce4504;
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; CAN94667.1; -; Genomic_DNA.
DR RefSeq; WP_012237136.1; NC_010162.1.
DR AlphaFoldDB; A9F8L0; -.
DR SMR; A9F8L0; -.
DR STRING; 448385.sce4504; -.
DR PRIDE; A9F8L0; -.
DR EnsemblBacteria; CAN94667; CAN94667; sce4504.
DR KEGG; scl:sce4504; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_7; -.
DR OMA; VLDCVPM; -.
DR OrthoDB; 128102at2; -.
DR BioCyc; SCEL448385:SCE_RS23120-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..799
FT /note="Lon protease 4"
FT /id="PRO_0000396600"
FT DOMAIN 15..202
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 595..776
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 682
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 725
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 356..363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 799 AA; 85866 MW; B9330AB59000EBA5 CRC64;
MSQLRSGASA PRSPFPLLPL RTGVLFPGTV LTLPVGRPRS VALLNAVHAG DVIGVIAQRD
PKREDPRRED LHDIGTFARV VDISRVSNGY RLVIEGLDRF ALSALVETEP TWRAEGTLAP
EFLGDAEEAR LLAASLRERA REVGPKTGTN LAEIAATSRA EPGVFADQVA GALGLPTEKE
MEVLSELRVV PRLQRVAGLL AEASALADLK KKIDGDVRRE LGKGQREVIL REQLRAIQKE
LAGGEEGEDE LSALRRRLDE AGLPEEARAV ADRELRRLES VGPQSAEHNV IRTYLEWIAD
LPWSARAEVK DDLDAVKAKL DEEHRGLDDV KRRILEHMAV LKLTGKARAT ILCFAGPPGV
GKTSLGQSIA DATGRPFVRI SLGGVHDEAE LRGHRRTYVG ALPGRIVHAL KKAKVKNPIV
LLDEVDKLGA GWRGSPEAAL LEVLDPEQNR TFVDHYLELP FDLSEVVFLC TVNDLGALSA
PLRDRLEVIE LSGYTPDEKI AIARSHLVPK QLKEHAIDPG SLSITDEALA AIVRDYTREA
GVRQLGREIK KLCRAVALEI ARAADGKAPR VVVEASDLGT YLGKVRFFSD VAERTSVAGV
ATGLAWTPVG GDILFIETSR MPGKGRVEIT GQLGDVMKES AKAALTYVRS HAIELGVDTA
KLEAEDLHIH VPAGGVPKDG PSAGVTMFTA LTSLLSARRV RSDTAMTGEC TLRGRVLPVG
GIKSKVLAAH RAGIKRVVLP QKNARDAEEI PKEVRAELEL IFVEDMSQVI AAALEEAPIE
AAGTGGVTGA AAGEPAAAA
