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Database: UniProt
Entry: Q87G24_VIBPA
LinkDB: Q87G24_VIBPA
Original site: Q87G24_VIBPA 
ID   Q87G24_VIBPA            Unreviewed;       786 AA.
AC   Q87G24;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   OrderedLocusNames=VPA1493 {ECO:0000313|EMBL:BAC62836.1};
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC62836.1, ECO:0000313|Proteomes:UP000002493};
RN   [1] {ECO:0000313|EMBL:BAC62836.1, 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; BA000032; BAC62836.1; -; Genomic_DNA.
DR   RefSeq; NP_801003.1; NC_004605.1.
DR   RefSeq; WP_005478132.1; NC_004605.1.
DR   AlphaFoldDB; Q87G24; -.
DR   GeneID; 1192189; -.
DR   KEGG; vpa:VPA1493; -.
DR   PATRIC; fig|223926.6.peg.4418; -.
DR   eggNOG; COG1067; Bacteria.
DR   HOGENOM; CLU_014785_0_1_6; -.
DR   Proteomes; UP000002493; Chromosome 2.
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; 1.10.8.60; -; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR041699; AAA_32.
DR   InterPro; IPR046844; Lon-like_helical.
DR   InterPro; IPR008269; Lon_proteolytic.
DR   InterPro; IPR027065; Lon_Prtase.
DR   InterPro; IPR046843; LonB_AAA-LID.
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:SF46; ARCHAEAL LON PROTEASE; 1.
DR   PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR   Pfam; PF13654; AAA_32; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   Pfam; PF20436; LonB_AAA-LID; 1.
DR   Pfam; PF20437; LonC_helical; 1.
DR   PRINTS; PR00830; ENDOLAPTASE.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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          562..757
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   ACT_SITE        652
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        695
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   786 AA;  88102 MW;  DBBBE466C6F85DEF CRC64;
     MAILRLEPQQ LYSVADLENM PCKSTKELPP IDEIVGQERA QKAVEFAMSI KEKGYNIYAI
     GQNGLGKRTM ILRYLNRHQH DADALFDWCY VANFEDTRTP KVLKLPCGIG NKLRVDIEAL
     MGKLLNALPL AFDNEMYFSR ADRLKNQLAN KQQNELDRIS REAKEHGISL TITSQGDYQF
     VAMNGDELHT EESFDALSKK EQEQFSDSID ALEVSLRSMV RELTEWEDTY SDKIKKLNDE
     VTLDVITHFI KKLKVDYSEY SEIKTYLTEL QKDIVENADI FLDQSGEQGE IAAASLDKKL
     PRRYKVNVLV SRNNSDFPIV VEENPNYHSL FGSIETATFK GTVFTDFSLI RAGSLHKANG
     GVLLMDAQKV LEQPYVWDGL KRALRARQLS FTSLEKEVTL TGAVSLDPEP IPLDIKIILF
     GDYRTYQLLQ HYDPEFSELF RVTADFEDEM KRTPESELHY ARFISSVVHD NNMLHCDRKA
     IARIIEYSSR LSGDQSKLSL HSANIANLLR ESNYVARQAN SNMIRIGHVE EAMKNQEMRV
     SRLRDSVMET FLNGTTLILT EGSAIGQVNA LSVLSTSDYM FGAPNRITAT TCYGDGDVID
     IERSVDLGGS IHSKGVMILS AYLSSVFGKT ARVPLTTTIT FEQSYGGVDG DSASMAEFCA
     VVSAFSKQPN RQDIAITGSM NQFGEAQPIG GVNEKIEGFY DVCVIKGRHS GQGVIIPRSN
     VHNLMLRADI VKAVEKGEFH IWAIDHVTEA IELFTGKVAG EPTDEGSYPI DTIFGLAQAK
     LNSLRK
//
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