LON_PHEZH
ID LON_PHEZH Reviewed; 792 AA.
AC B4RI01;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=PHZ_p0033;
OS Phenylobacterium zucineum (strain HLK1).
OG Plasmid pHLK1.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=450851;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLK1;
RX PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT "Complete genome of Phenylobacterium zucineum - a novel facultative
RT intracellular bacterium isolated from human erythroleukemia cell line
RT K562.";
RL BMC Genomics 9:386-386(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; CP000748; ACG79976.1; -; Genomic_DNA.
DR RefSeq; WP_012520276.1; NC_011143.1.
DR AlphaFoldDB; B4RI01; -.
DR SMR; B4RI01; -.
DR STRING; 450851.PHZ_p0033; -.
DR EnsemblBacteria; ACG79976; ACG79976; PHZ_p0033.
DR KEGG; pzu:PHZ_p0033; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_5; -.
DR OMA; MVNIEDK; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000001868; Plasmid pHLK1.
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; Plasmid; Protease;
KW Reference proteome; Serine protease; Stress response.
FT CHAIN 1..792
FT /note="Lon protease"
FT /id="PRO_0000396592"
FT DOMAIN 16..209
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 597..778
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 684
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 727
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 361..368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 792 AA; 86499 MW; C7C4CEAF052C084F CRC64;
MNGEQSANGA RTLPDDAVVV VPVSNVIFPG VVFPIVLDRP SAVAAAQQAL REQHPLVLVL
QQDVQAPDPG PQSLHRMGTL ANVLRYVTGP DGAPHVACQG VERFEIDEWV EGFPFLVARG
RRIPEPEAEG AAIEARFLHL RSQALEALQL LPQSPPGELV AAVEGASSPA ALADLVAAYL
DLQPPEKQQI LETIDLEARL DKVSAFLAQR LEVLRLTSEI AQRTRQSLGE RQRETLLREQ
MAAIQRELGE GEREELVELE AAIENAGMPE EVVQQARKEL RRLARTPEAA AEYGMVRTYL
EWLVELPWGV PEAAPIDLAE ARRILDEDHF GLEKIKQRII EHLAVRRLAP EGKAPILCFV
GPPGVGKTSL GQSIARAMHR PFVRVSLGGV HDESEIRGHR RTYVGALPGN IIQAIRKAGR
RDCVMMLDEI DKMSAGIHGD PSAALLEVLD PEQNVAFRDN YLAVPFDLSR VVFIATANML
DTIPGPLRDR MEVIQLSGYT AGEKRQIAER YLVRRQLEAN GLTAEQVQIE PAALETLIAR
YTREAGVRSL EREIGRLLRH VAVRFAEGHT EPVRIGPTNL EPILGPPRVE NEVAMRTSVP
GVATGLAWTP VGGEILFIEA TRTPGDGRLI LTGQLGEVMR ESAQTALSLV KSRAEALGVT
PSLFKESDIH IHVPAGATPK DGPSAGVAMT MALISLLTDR TVRSDTAMTG EISLRGLVLP
VGGIKEKVVA AATAGVRRVL LPARNRADER DIPEETRQTL ELIWLERIED AIEAGLDPRR
GDVRQTQVRA AS
