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Database: UniProt
Entry: A0A233HD87_9VIBR
LinkDB: A0A233HD87_9VIBR
Original site: A0A233HD87_9VIBR 
ID   A0A233HD87_9VIBR        Unreviewed;       170 AA.
AC   A0A233HD87;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Hydrolase {ECO:0000313|EMBL:OXX59482.1};
GN   ORFNames=B9J89_21105 {ECO:0000313|EMBL:OXX59482.1};
OS   Vibrio sp. V15_P4S5T153.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1938669 {ECO:0000313|EMBL:OXX59482.1, ECO:0000313|Proteomes:UP000215241};
RN   [1] {ECO:0000313|EMBL:OXX59482.1, ECO:0000313|Proteomes:UP000215241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V15_P4S5T153 {ECO:0000313|EMBL:OXX59482.1,
RC   ECO:0000313|Proteomes:UP000215241};
RA   Vazquez-Rosas-Landa M.;
RT   "High clonality and local adaptation shapes Vibrionaceae linages within an
RT   endangered oasis.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-
CC       anchor {ECO:0000256|ARBA:ARBA00004635}.
CC   -!- SIMILARITY: Belongs to the peptidase C40 family.
CC       {ECO:0000256|ARBA:ARBA00007074}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OXX59482.1}.
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DR   EMBL; NDIJ01000024; OXX59482.1; -; Genomic_DNA.
DR   RefSeq; WP_017042506.1; NZ_NDIJ01000024.1.
DR   AlphaFoldDB; A0A233HD87; -.
DR   Proteomes; UP000215241; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR   InterPro; IPR000064; NLP_P60_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   PANTHER; PTHR47360; MUREIN DD-ENDOPEPTIDASE MEPS/MUREIN LD-CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR47360:SF3; MUREIN DD-ENDOPEPTIDASE MEPS_MUREIN LD-CARBOXYPEPTIDASE; 1.
DR   Pfam; PF00877; NLPC_P60; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS51935; NLPC_P60; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OXX59482.1};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT   DOMAIN          43..164
FT                   /note="NlpC/P60"
FT                   /evidence="ECO:0000259|PROSITE:PS51935"
SQ   SEQUENCE   170 AA;  18989 MW;  4E6ABCB53FA54D4C CRC64;
     MIKSPILFAL SITSVLTGCV GSPISSNSGP TYVTQEEILS IVQDKDDGLG TVFQRWQGVP
     YRLGGETLNG VDCSAFVQIA FKDVWQIPLP RTTRSQSQTG FEVNYQNAQR GDLVFFRTSR
     TSNHVGVYLG DKKFMHASTS KGVMISRIDN PYWASKFWQF RRIISPPNSD
//
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