ID   Q87PC7_VIBPA            Unreviewed;       545 AA.
AC   Q87PC7;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   OrderedLocusNames=VP1590 {ECO:0000313|EMBL:BAC59853.1};
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC59853.1, ECO:0000313|Proteomes:UP000002493};
RN   [1] {ECO:0000313|EMBL:BAC59853.1, ECO:0000313|Proteomes:UP000002493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01122};
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01122}.
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DR   EMBL; BA000031; BAC59853.1; -; Genomic_DNA.
DR   RefSeq; NP_797969.1; NC_004603.1.
DR   RefSeq; WP_005457453.1; NC_004603.1.
DR   AlphaFoldDB; Q87PC7; -.
DR   MEROPS; S16.A10; -.
DR   GeneID; 1189097; -.
DR   KEGG; vpa:VP1590; -.
DR   PATRIC; fig|223926.6.peg.1516; -.
DR   eggNOG; COG1067; Bacteria.
DR   HOGENOM; CLU_014785_2_0_6; -.
DR   Proteomes; UP000002493; Chromosome 1.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR041699; AAA_32.
DR   InterPro; IPR008269; Lon_proteolytic.
DR   InterPro; IPR027065; Lon_Prtase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10046:SF49; LON PROTEASE HOMOLOG-RELATED; 1.
DR   Pfam; PF13654; AAA_32; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   PRINTS; PR00830; ENDOLAPTASE.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000002493};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   DOMAIN          310..507
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   ACT_SITE        402
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        445
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   545 AA;  60555 MW;  E94F5D19606BD8C7 CRC64;
     MNQLNWKDVT PSFEQYEDIL KSASSLPKKK FVELQPRLLA TVERFKKIKG LTRVLVINCA
     DNTVYRKFIC DVVTDGLEPT IMTESLDAKL LFDRYSVDLK GDVVVEAGLL SKANGGYLIL
     PANLILANPG YWPSIKSAIQ GKPVNPLNVS PTRLPILTAD EKEFDVKIIV TGDRNQLADL
     EYVDEDFSTG LTMYTEVEED IHLSASNLEL YVGLVNWICS EYGFPSLDDG AFQRLLLAGM
     RLTEDQHYLP LGVMWHCQLL SLAAQFSDQN IIDYVAIDKA IDDKYYRESY LPQRAVYDIL
     DGQVIIETTG EQIGQINGLT VIDMAGHPVS YGEPARISCV IHFGDGDISD VERKAELGGN
     LHAKGMMIMQ AFLSSALNLD EPLPYSASIV FEQSYSEVDG DSASLAELCC LVSALSESPV
     NQQIAVTGAV DQFGRVQAVG GLNEKIEGFY QVCKHQGFTG HQGVIMPKSN LKHLALHKDV
     IESIKNGEFH IWSVSTVDEA IPILMGKSFR GEDDSVIGKI AERIENFERH EHPEGIVQRI
     KNWFV
//