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
//