LON_VIBPA
ID LON_VIBPA Reviewed; 783 AA.
AC P74956;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 137.
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}; Synonyms=lonS;
GN OrderedLocusNames=VP0919;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BB22;
RX PubMed=8981986; DOI=10.1128/jb.179.1.107-114.1997;
RA Stewart B.J., Enos-Berlage J.L., McCarter L.L.;
RT "The lonS gene regulates swarmer cell differentiation of Vibrio
RT parahaemolyticus.";
RL J. Bacteriol. 179:107-114(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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). Regulates swarmer cell
CC differentiation of V.parahaemolyticus. {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.
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}.
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; U66708; AAC44747.1; -; Genomic_DNA.
DR EMBL; BA000031; BAC59182.1; -; Genomic_DNA.
DR RefSeq; NP_797298.1; NC_004603.1.
DR RefSeq; WP_005493728.1; NC_004603.1.
DR AlphaFoldDB; P74956; -.
DR SMR; P74956; -.
DR STRING; 223926.28805906; -.
DR MEROPS; S16.001; -.
DR PRIDE; P74956; -.
DR EnsemblBacteria; BAC59182; BAC59182; BAC59182.
DR GeneID; 1188417; -.
DR KEGG; vpa:VP0919; -.
DR PATRIC; fig|223926.6.peg.871; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_6; -.
DR OMA; GAWQVVD; -.
DR Proteomes; UP000002493; Chromosome 1.
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; 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.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW Reference proteome; Serine protease; Stress response.
FT CHAIN 1..783
FT /note="Lon protease"
FT /id="PRO_0000076147"
FT DOMAIN 11..201
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 591..772
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 678
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 721
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 355..362
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT CONFLICT 136
FT /note="Q -> P (in Ref. 1; AAC44747)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="R -> P (in Ref. 1; AAC44747)"
FT /evidence="ECO:0000305"
FT CONFLICT 760
FT /note="Q -> R (in Ref. 1; AAC44747)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 783 AA; 87812 MW; 723A8A81BC501778 CRC64;
MNLERSERIE IPVLPLRDVV VYPHMVIPLF VGREKSISCL ETAMETNKQV LLVAQKQADT
DEPTVDDLFE VGTVATILQL LKLPDGTVKV LVEGQQRAKI NHFKESDFFL AEAEFIVTPE
LDEREQEVIV RSAINQFEGF IKLNKKIPPE VLTSLNGIDE AARLADTIAA HMPLKLVDKQ
QVLEIIDVTE RLEFLMGQME SEIDLLQVEK RIRGRVKKQM EKSQREYYLN EQMKAIQKEL
GEMEDAPDEF ETLQKKIDES KMPQEAREKT EQELQKLKMM SPMSAEATVV RSYIDWMVSV
PWTKRSKVKK NLAKAEEILN EDHYGLERVK ERILEYLAVQ NRINKLKGPI LCLVGPPGVG
KTSLGRSIAS ATGRKYVRMA LGGVRDEAEI RGHRRTYIGS LPGKLIQKMS KVGVKNPLFL
LDEIDKMSSD MRGDPASALL EVLDPEQNNS FNDHYLEVDY DLSDVMFVAT SNSMNIPGPL
LDRMEVIRLS GYTEDEKLNI AKRHLVEKQV QRNGLKPNEI VIEDSAIIGI IRYYTREAGV
RGLEREISKI CRKAVKNILL DKDIKSVTVT MDNLKEYLGV QRFDYGKADE SNRIGQVTGL
AWTEVGGDLL TIETQSMPGK GKLTQTGSLG DVMQESIQAA MTVVRSRADK LGINSDFYEK
KDIHVHVPEG ATPKDGPSAG TAMCTALVSA LTGNPVKAEV AMTGEITLRG EVLPIGGLKE
KLLAAHRGGI KTVLIPKDNE RDLEEIPENV IADLQVIPVQ WIDEVLKVAL ERDPTGVEFE
AKK
