ID   Q87LS1_VIBPA            Unreviewed;       947 AA.
AC   Q87LS1;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=Protease, insulinase family {ECO:0000313|EMBL:BAC60803.1};
GN   OrderedLocusNames=VP2540 {ECO:0000313|EMBL:BAC60803.1};
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC60803.1, ECO:0000313|Proteomes:UP000002493};
RN   [1] {ECO:0000313|EMBL:BAC60803.1, 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   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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; BA000031; BAC60803.1; -; Genomic_DNA.
DR   RefSeq; NP_798919.1; NC_004603.1.
DR   RefSeq; WP_011106066.1; NC_004603.1.
DR   AlphaFoldDB; Q87LS1; -.
DR   GeneID; 1190055; -.
DR   KEGG; vpa:VP2540; -.
DR   PATRIC; fig|223926.6.peg.2437; -.
DR   eggNOG; COG0612; Bacteria.
DR   HOGENOM; CLU_007487_0_1_6; -.
DR   Proteomes; UP000002493; Chromosome 1.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   PANTHER; PTHR43690:SF35; NON-CATALYTIC MEMBER OF PEPTIDASE SUBFAMILY M16B-RELATED; 1.
DR   Pfam; PF00675; Peptidase_M16; 2.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:BAC60803.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002493};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..947
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004304501"
FT   DOMAIN          65..150
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          215..390
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          535..641
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          682..857
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   947 AA;  105800 MW;  280C6F4A5804EC92 CRC64;
     MRMFWVGACS LLVITGCASN SPVSSLPKGV TFVESSKAED GKVKIPYQKY KLDNGLTVIL
     APEGSDPLVH VDVTYHVGSA REEIGKSGFA HFFEHMMFQG SENVGDQEHF KIITEAGGTL
     NGTTNRDRTN YFETVPANQL EKMLWLESDR MGFLLDAVSQ RKFEIQRSTV KNERAQRYDN
     RPYGLIWERM SEALYPEGHP YSWQTIGYVE DLERVDVNDL KAFFLRWYGP NNATITIGGD
     LDVEQTLAWV NKYFGSIPRG PEVENAPKQP AKLQEDKYIT LEDRIQQPMV MIAWPTTYSG
     EESQASLDTL SEVLGGGTNS VLYQDLVKTQ KAVDAGSFHD CAELACNFYV YAMGDSGDKG
     DLSTLYGELM KSMSKFAEKG VTDDRLEQLK GKAEADAIFA LESVKGKVTQ LASNETFFGQ
     PDLIEKQLEQ IRAVTPQSVE KVYQNFIQGK SKVTLSVVPK GKTDLAVKSA TFTTPERTLP
     EYKKITDDQL AYRRATDNFD RSVQPPVGEP VKATMPELYN VHFDNGSELL GTVSNETPTV
     MMQFSLPAGT RFVEKGKEGL AQLTAAMLQE GTTKRSVEQI QAELDKLGSM ISVDATGYTT
     NISVSSLEKN LEPTLKIVEE MLLSPAFKQE DFDRVKMQAL EGLVYEHQNP SWMASQASRQ
     VLYGDSVFAR PKDGTQAGVS ALTLDDVREF YAKHYTPQSA QVVVVGDIAK QDIEQKLAFW
     AEWKDEAAPL YAPQTIPALG EQKIHLVDKP GAPQSVVMMV RQGMPYDATG DFYLSQLANF
     NLAGNFNSRI NQNLREDKGY TYGAYGYFSG NPETGSVVFT AQVRADSTVA SIIEMENELN
     EYAQSGMTDE EMKFMRQAVG QKDALKYETP TQKAELISDI LKYNLDQDYL QQRNAIVEKV
     DKQTLNALAQ KWFDPNDYQI IVVGDAKSLR PQLEKLGKDV EELEIIR
//