LON1_BACSU
ID LON1_BACSU Reviewed; 774 AA.
AC P37945;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Lon protease 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01973};
GN Name=lon1 {ECO:0000255|HAMAP-Rule:MF_01973}; Synonyms=lonA;
GN OrderedLocusNames=BSU28200;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=168 / IS58;
RX PubMed=7961402; DOI=10.1128/jb.176.21.6518-6527.1994;
RA Riethdorf S., Voelker U., Gerth U., Winkler A., Engelmann S., Hecker M.;
RT "Cloning, nucleotide sequence, and expression of the Bacillus subtilis lon
RT gene.";
RL J. Bacteriol. 176:6518-6527(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA Emmerson P.T., Harwood C.R.;
RT "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT chromosome containing genes responsible for stress responses, the
RT utilization of plant cell walls and primary metabolism.";
RL Microbiology 142:3067-3078(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP STRUCTURE BY NMR OF 490-604.
RX PubMed=19636865; DOI=10.1007/s12104-007-9056-6;
RA Wang I., Lou Y.C., Lin Y.C., Lo S.C., Lee A.Y., Wu S.H., Chen C.;
RT "(1)H, (13)C and (15)N resonance assignments of alpha-domain for Bacillus
RT subtilis Lon protease.";
RL Biomol. NMR. Assign. 1:201-203(2007).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-209 IN COMPLEX WITH ADP, AND
RP SUBUNIT.
RX PubMed=20600124; DOI=10.1016/j.jmb.2010.06.030;
RA Duman R.E., Loewe J.;
RT "Crystal structures of Bacillus subtilis Lon protease.";
RL J. Mol. Biol. 401:653-670(2010).
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 (By similarity). Has been implicated in preventing
CC sigma(G) activity under non-sporulation conditions. {ECO:0000255|HAMAP-
CC 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 (By
CC similarity). Exists as a mixture of small oligomeric species in
CC solution. {ECO:0000255|HAMAP-Rule:MF_01973,
CC ECO:0000269|PubMed:20600124}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By heat shock. {ECO:0000255|HAMAP-Rule:MF_01973,
CC ECO:0000269|PubMed:7961402}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_01973}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X76424; CAA53984.1; -; Genomic_DNA.
DR EMBL; Z75208; CAA99540.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14780.1; -; Genomic_DNA.
DR PIR; I40421; I40421.
DR RefSeq; NP_390698.1; NC_000964.3.
DR RefSeq; WP_003229618.1; NZ_JNCM01000036.1.
DR PDB; 1X37; NMR; -; A=490-604.
DR PDB; 3M65; X-ray; 2.60 A; A/B=1-209.
DR PDB; 3M6A; X-ray; 3.40 A; A/B/C/D/E/F=240-774.
DR PDBsum; 1X37; -.
DR PDBsum; 3M65; -.
DR PDBsum; 3M6A; -.
DR AlphaFoldDB; P37945; -.
DR BMRB; P37945; -.
DR SMR; P37945; -.
DR IntAct; P37945; 2.
DR MINT; P37945; -.
DR STRING; 224308.BSU28200; -.
DR MEROPS; S16.001; -.
DR PaxDb; P37945; -.
DR PRIDE; P37945; -.
DR EnsemblBacteria; CAB14780; CAB14780; BSU_28200.
DR GeneID; 937486; -.
DR KEGG; bsu:BSU28200; -.
DR PATRIC; fig|224308.179.peg.3063; -.
DR eggNOG; COG0466; Bacteria.
DR InParanoid; P37945; -.
DR OMA; GAWQVVD; -.
DR PhylomeDB; P37945; -.
DR BioCyc; BSUB:BSU28200-MON; -.
DR BRENDA; 3.4.21.53; 658.
DR EvolutionaryTrace; P37945; -.
DR Proteomes; UP000001570; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding;
KW Protease; Reference proteome; Serine protease; Stress response.
FT CHAIN 1..774
FT /note="Lon protease 1"
FT /id="PRO_0000076116"
FT DOMAIN 9..200
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 590..771
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 677
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 720
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 354..361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT STRAND 5..16
FT /evidence="ECO:0007829|PDB:3M65"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:3M65"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:3M65"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:3M65"
FT STRAND 46..55
FT /evidence="ECO:0007829|PDB:3M65"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:3M65"
FT STRAND 68..80
FT /evidence="ECO:0007829|PDB:3M65"
FT STRAND 86..103
FT /evidence="ECO:0007829|PDB:3M65"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:3M65"
FT HELIX 124..155
FT /evidence="ECO:0007829|PDB:3M65"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:3M65"
FT HELIX 175..182
FT /evidence="ECO:0007829|PDB:3M65"
FT HELIX 187..207
FT /evidence="ECO:0007829|PDB:3M65"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:3M6A"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 264..274
FT /evidence="ECO:0007829|PDB:3M6A"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:3M6A"
FT TURN 284..287
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 288..298
FT /evidence="ECO:0007829|PDB:3M6A"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 318..321
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 326..341
FT /evidence="ECO:0007829|PDB:3M6A"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:3M6A"
FT STRAND 349..359
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 360..371
FT /evidence="ECO:0007829|PDB:3M6A"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 404..409
FT /evidence="ECO:0007829|PDB:3M6A"
FT STRAND 413..425
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:3M6A"
FT TURN 444..448
FT /evidence="ECO:0007829|PDB:3M6A"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:3M6A"
FT STRAND 465..469
FT /evidence="ECO:0007829|PDB:3M6A"
FT TURN 473..475
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 478..483
FT /evidence="ECO:0007829|PDB:3M6A"
FT STRAND 484..488
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 494..503
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 505..512
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 517..519
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 524..534
FT /evidence="ECO:0007829|PDB:3M6A"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 541..559
FT /evidence="ECO:0007829|PDB:3M6A"
FT STRAND 560..562
FT /evidence="ECO:0007829|PDB:1X37"
FT TURN 570..573
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 574..577
FT /evidence="ECO:0007829|PDB:3M6A"
FT TURN 586..588
FT /evidence="ECO:0007829|PDB:3M6A"
FT STRAND 592..602
FT /evidence="ECO:0007829|PDB:3M6A"
FT STRAND 605..618
FT /evidence="ECO:0007829|PDB:3M6A"
FT STRAND 622..627
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 630..643
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 648..650
FT /evidence="ECO:0007829|PDB:3M6A"
FT TURN 657..659
FT /evidence="ECO:0007829|PDB:3M6A"
FT STRAND 661..666
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 672..678
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 679..690
FT /evidence="ECO:0007829|PDB:3M6A"
FT STRAND 710..712
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 717..726
FT /evidence="ECO:0007829|PDB:3M6A"
FT STRAND 730..735
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 736..744
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 747..750
FT /evidence="ECO:0007829|PDB:3M6A"
FT STRAND 757..760
FT /evidence="ECO:0007829|PDB:3M6A"
FT HELIX 761..768
FT /evidence="ECO:0007829|PDB:3M6A"
SQ SEQUENCE 774 AA; 86607 MW; BE339D896FCEF533 CRC64;
MAEELKRSIP LLPLRGLLVY PTMVLHLDVG RDKSVQALEQ AMMHDHMIFL ATQQDISIDE
PGEDEIFTVG TYTKIKQMLK LPNGTIRVLV EGLKRAHIVK YNEHEDYTSV DIQLIHEDDS
KDTEDEALMR TLLDHFDQYI KISKKISAET YAAVTDIEEP GRMADIVASH LPLKLKDKQD
ILETADVKDR LNKVIDFINN EKEVLEIEKK IGQRVKRSME RTQKEYYLRE QMKAIQKELG
DKEGKTGEVQ TLTEKIEEAG MPDHVKETAL KELNRYEKIP SSSAESSVIR NYIDWLVALP
WTDETDDKLD LKEAGRLLDE EHHGLEKVKE RILEYLAVQK LTKSLKGPIL CLAGPPGVGK
TSLAKSIAKS LGRKFVRISL GGVRDESEIR GHRRTYVGAM PGRIIQGMKK AGKLNPVFLL
DEIDKMSSDF RGDPSSAMLE VLDPEQNSSF SDHYIEETFD LSKVLFIATA NNLATIPGPL
RDRMEIINIA GYTEIEKLEI VKDHLLPKQI KEHGLKKSNL QLRDQAILDI IRYYTREAGV
RSLERQLAAI CRKAAKAIVA EERKRITVTE KNLQDFIGKR IFRYGQAETE DQVGVVTGLA
YTTVGGDTLS IEVSLSPGKG KLILTGKLGD VMRESAQAAF SYVRSKTEEL GIEPDFHEKY
DIHIHVPEGA VPKDGPSAGI TMATALVSAL TGRAVSREVG MTGEITLRGR VLPIGGLKEK
ALGAHRAGLT TIIAPKDNEK DIEDIPESVR EGLTFILASH LDEVLEHALV GEKK
