LON_ACIB3
ID LON_ACIB3 Reviewed; 809 AA.
AC B7GXS7;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Lon protease {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 {ECO:0000255|HAMAP-Rule:MF_01973};
GN Name=lon {ECO:0000255|HAMAP-Rule:MF_01973}; OrderedLocusNames=ABBFA_002579;
OS Acinetobacter baumannii (strain AB307-0294).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=557600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB307-0294;
RX PubMed=18931120; DOI=10.1128/jb.00834-08;
RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA Bonomo R.A., Gill S.R.;
RT "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT baumannii.";
RL J. Bacteriol. 190:8053-8064(2008).
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; CP001172; ACJ57053.1; -; Genomic_DNA.
DR RefSeq; WP_001292274.1; NZ_CP001172.1.
DR AlphaFoldDB; B7GXS7; -.
DR SMR; B7GXS7; -.
DR MEROPS; S16.001; -.
DR PRIDE; B7GXS7; -.
DR HOGENOM; CLU_004109_4_3_6; -.
DR OMA; GAWQVVD; -.
DR Proteomes; UP000006924; 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 Serine protease; Stress response.
FT CHAIN 1..809
FT /note="Lon protease"
FT /id="PRO_0000396531"
FT DOMAIN 20..214
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 606..787
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 693
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 736
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 369..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 809 AA; 90128 MW; FBCD52097C9505EF CRC64;
MSELIMNEKT DLEPQVPSVL PLLALRDVVV YPHMQIALFV GREKSINAVD VARNSDNLVF
VVAQKDSLTE EIDHDNLYQY GTVAKIVQVV NHENDENCIK VLIEGLHRSK LKKIIDEDSY
LTAEHELSPM TINVDKATQE TRLQELRNLF AQYAEAKLRN ARELVAAANK IEDLLQLMFF
VATRVPLNIE IKQKFLEYDE FEAHLQELMN YLMNQSAEQQ IEQTLHDSVK RQMEKNQREY
FLNEKMKVIQ RELSDMNGGA EDDVAEIEKR LAEADLPEHV RKKAEAEFRK LKAMQPASSE
AAVVRNYLEV ILDTPWNKAS KVSINLNKAQ EILDADHYGL DDVKDRIVEY LAVQSRVKKL
KGPILCLVGP PGVGKTSLGE SVAKATGREF VRMALGGVRD EAEIRGHRRT YIGAMPGKIV
QSLTKVGVKN PLFLLDEIDK MAQDYRGDPA SALLEVLDPS QNSKFNDHYL DLDLDLSEVM
FICTANSMNI PEALLDRMEV IRLPGYTEDE KVNIAERYLV PKAIKNNGLR PKELTIHEEA
IRDIVQRYTR EAGVRNLERE VSKIARKVVK EAVSKKSKNL QLDVTSANLP EYLGPHKFDF
GMAEDEAQVG RVNGLAWTSV GGELLTIEVA AVKGKGKFIT TGSLGDVMKE SITTAMTVVR
TRADELGIEA SRFEETDVHV HLPEGATPKD GPSAGLALTT ALVSAFTGIA IRPDIAMTGE
TSLGGRAMRI GGLKEKLLAA HRGGIKLVFI PQDNVRDLAE IPDNVKEGLE IKAVKSIDEI
LPLALTSMPK PLPKTPIVKP VEGSKAARH
