ID   G5R0A5_SALSE            Unreviewed;       680 AA.
AC   G5R0A5;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Dipeptidyl carboxypeptidase 2 {ECO:0000313|EMBL:EHC88439.1};
GN   ORFNames=LTSESEN_2674 {ECO:0000313|EMBL:EHC88439.1};
OS   Salmonella enterica subsp. enterica serovar Senftenberg str. A4-543.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=913082 {ECO:0000313|EMBL:EHC88439.1, ECO:0000313|Proteomes:UP000005065};
RN   [1] {ECO:0000313|EMBL:EHC88439.1, ECO:0000313|Proteomes:UP000005065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A4-543 {ECO:0000313|EMBL:EHC88439.1,
RC   ECO:0000313|Proteomes:UP000005065};
RX   PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA   den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA   Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA   Furtado M.R., Wiedmann M.;
RT   "Genome sequencing reveals diversification of virulence factor content and
RT   possible host adaptation in distinct subpopulations of Salmonella
RT   enterica.";
RL   BMC Genomics 12:425-425(2011).
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}.
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:EHC88439.1}.
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DR   EMBL; AFCU01000875; EHC88439.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5R0A5; -.
DR   MEROPS; M03.005; -.
DR   PATRIC; fig|913082.3.peg.2057; -.
DR   BioCyc; SENT913082:G120J-387-MONOMER; -.
DR   Proteomes; UP000005065; Unassembled WGS sequence.
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:EHC88439.1};
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          229..676
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   680 AA;  77274 MW;  552E7D0625380F70 CRC64;
     MSTNPLLDQS MLPYQAPRFD RIKDCHYRPA FDEGVRQKRV EIEAIVNHPA APDFTNTLLA
     LEQSGALLSR VTSVFFAMTA AHTNDELQRL DEAFSAELAA LSNDIYLNSA LFARVDAVWQ
     QRHSLGLDDE SLRLVDVIHQ RFVLAGAQLA EEDKARLKVL NTESATLMSQ FNQRLLAASK
     AGGLAVDDAH CLAGLSPEER TVAAEAAREK GLEERWFIPL LNTTQQPALA TLRDRQTREN
     LFAASWTRAE KGDAHDTRAI VQRLVEIRRC QAKLLGFPNY AAWKMADQMA KTPQAALSFM
     RGIVPPARQR VLNEQAEIQN VIDGEQGGYT VQAWDWMFYA EQVRREKYAL DEAQLKPYFA
     LNTVLQEGVF WTANQLFGIT FVERFDIPVY HPDVRVWEIF DSDGVGMALF YGDFFARDSK
     SGGAWMGNFV EQSTLNETRP VIYNVCNYQK PVDGQPALLL WDDVITLFHE FGHTLHGLFA
     VQRYATLSGT NTPRDFVEFP SQINEHWASH PRVFERYARH VDSGEKMPAD LQEKMRKASL
     FNKGYDMTEL LGAALLDMRW HMLEESVAEQ SVAEFEQQAL AAEHLDLPAV PPRYRSSYFA
     HIFGGGYAAG YYAYLWTQML ADDGYQWFVE QGGLTRENGQ RFRDAILSRG NSTDLETLYS
     AWRGHEPHID PMLQYRGLDR
//