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Entry: S5MVT4_SALBN
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ID   S5MVT4_SALBN            Unreviewed;       679 AA.
AC   S5MVT4;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Dipeptidyl carboxypeptidase Dcp {ECO:0000313|EMBL:AGR58719.1};
GN   ORFNames=A464_1533 {ECO:0000313|EMBL:AGR58719.1};
OS   Salmonella bongori N268-08.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1197719 {ECO:0000313|EMBL:AGR58719.1, ECO:0000313|Proteomes:UP000015042};
RN   [1] {ECO:0000313|EMBL:AGR58719.1, ECO:0000313|Proteomes:UP000015042}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N268-08 {ECO:0000313|EMBL:AGR58719.1,
RC   ECO:0000313|Proteomes:UP000015042};
RA   Marti R., Hagens S., Loessner M.J., Klumpp J.;
RT   "Genome sequence of Salmonella bongori N268-08 - a rare clinical isolate.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; CP006608; AGR58719.1; -; Genomic_DNA.
DR   RefSeq; WP_020844207.1; NC_021870.1.
DR   AlphaFoldDB; S5MVT4; -.
DR   MEROPS; M03.005; -.
DR   GeneID; 66755954; -.
DR   KEGG; sbz:A464_1533; -.
DR   PATRIC; fig|1197719.3.peg.1528; -.
DR   eggNOG; COG0339; Bacteria.
DR   HOGENOM; CLU_001805_4_0_6; -.
DR   Proteomes; UP000015042; Chromosome.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06456; M3A_DCP; 1.
DR   Gene3D; 1.10.1370.40; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR034005; M3A_DCP.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:AGR58719.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          232..674
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   679 AA;  77305 MW;  2D5EB4913CF6A84F CRC64;
     MSTNPFLDQS MLPYQAPRFD RIKECHYRPA FDEGVRQKRA EIEAIVNHPA TPDFTNTFLA
     LEQSGALLSR VTSVFFAMTA AHTNAALQRL DEAFSAELAA LSTDIYLNNA LFARVDTVWR
     QRHSLGLDNE SLRLVEVIHQ RFVLAGAQLA DEDKARLKAL NTEAATLMSQ FNQRLLAANK
     AGGLTVDDAH CLEGLSPQEI AVAAGAAREK GLEKRWRIPL LNTTQQPALA VLRDRQTREN
     LFMASWSRAE KDDAHDTRAI IQRLVEIRRC QAKLLGFPNY AAWKIADQMA KTPEAALDFM
     RSIVPPARQR VLNEQAEIQS VIDEQDGFPV QPWDWMFYAE QVRREKYALD EAQLKPYFAL
     NNVLQEGIFW TANQLFGITF VERYDIPVYH PDVRVWEILD HDGVGMALFY GDFFARDSKS
     GGAWMGNFVE QSTLNDTRPV IYNVCNYQKP VDGQPALLLW DDVITLFHEF GHTLHGLFAV
     QRYATLSGTN TPRDFVEFPS QINEHWASHP QVFERYARHV ESGEKMPADL QERMRQASLF
     NKGYDMAELL GAALLDMRWH MLEDSVAEQS VAGFEHQALA AEHLDLPAVP PRYRSSYFAH
     IFGGGYAAGY YAYLWTQMLA DDGYQWFVEQ GGLTRENGQR FRDAILSQGN SADLDRLYSA
     WRGHEPHIGP MLRYRGLHH
//
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