ID   Q0T4N4_SHIF8            Unreviewed;       681 AA.
AC   Q0T4N4;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   SubName: Full=Dipeptidyl carboxypeptidase II {ECO:0000313|EMBL:ABF03731.1};
GN   Name=dcp {ECO:0000313|EMBL:ABF03731.1};
GN   OrderedLocusNames=SFV_1552 {ECO:0000313|EMBL:ABF03731.1};
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384 {ECO:0000313|EMBL:ABF03731.1, ECO:0000313|Proteomes:UP000000659};
RN   [1] {ECO:0000313|EMBL:ABF03731.1, ECO:0000313|Proteomes:UP000000659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401 {ECO:0000313|EMBL:ABF03731.1,
RC   ECO:0000313|Proteomes:UP000000659};
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
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; CP000266; ABF03731.1; -; Genomic_DNA.
DR   RefSeq; WP_005068122.1; NC_008258.1.
DR   AlphaFoldDB; Q0T4N4; -.
DR   MEROPS; M03.005; -.
DR   KEGG; sfv:SFV_1552; -.
DR   HOGENOM; CLU_001805_4_0_6; -.
DR   Proteomes; UP000000659; 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:ABF03731.1};
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          230..678
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   681 AA;  77503 MW;  C737E467226E8401 CRC64;
     MTTMNPFLVQ STLPYLAPHF DQIANHHYRP AFDEGMQQKR AEIAAIALNP QTPDFNNTIL
     ALEQSGELIT RVTSVFFAMT AAHTNDELQR LDEQFSAELA ELANDIYLNG ELFARVDAVW
     QRRESLGLDS ESIRLVEVIH QRFVLAGAKL AQADKAKLKV LNTEAATLTS QFNQRLLAAN
     KSGGLVVNDI AQLAGMSEQE IALAAEAARE KGLDNKWLIP LLNTTQQPAL AEMRDRATRE
     KLFIAGWTRA EKNDANDTRA IIQRLVEIRA QQAKLLGFPH YAAWKIADQM AKTPEAALNF
     MREIVPAARQ RASDELASIQ AVIDKQQGGF SAQPWDWAFY AEQVRREKFD LDEAQLKPYF
     ELNTVLNEGV FWTANQLFGI KFVERFDIPV YHPDVRVWEI FDHNGVGLAL FYGDFFARDS
     KSGGAWMGNF VEQSTLNETH PVIYNVCNYQ KPAAGEPALL LWDDVITLFH EFGHTLHGLF
     ARQRYATLSG TNTPRDFVEF PSQINEHWAT HPQVFARYAR HYQSGAAMPD ELQQKMRNAS
     LFNKGYEMSE LLSAALLDMR WHCLEENEAM QDVDDFELRA LVAENMDLPA IPPRYRSSYF
     AHIFGGGYAA GYYAYLWTQM LADDGYQWFV EQGGLTRENG QRFREAILSR GNSEDLERLH
     RQWRGKAPQI MPMLQHRGLN I
//