ID B2U1I5_SHIB3 Unreviewed; 681 AA.
AC B2U1I5;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE SubName: Full=Peptidyl-dipeptidase Dcp {ECO:0000313|EMBL:ACD08988.1};
DE EC=3.4.15.5 {ECO:0000313|EMBL:ACD08988.1};
GN Name=dcp {ECO:0000313|EMBL:ACD08988.1};
GN OrderedLocusNames=SbBS512_E1702 {ECO:0000313|EMBL:ACD08988.1};
OS Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=344609 {ECO:0000313|EMBL:ACD08988.1, ECO:0000313|Proteomes:UP000001030};
RN [1] {ECO:0000313|Proteomes:UP000001030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 3083-94 / BS512 {ECO:0000313|Proteomes:UP000001030};
RA Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA Jiang L., Ravel J., Sebastian Y.;
RT "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL Submitted (MAY-2008) 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; CP001063; ACD08988.1; -; Genomic_DNA.
DR RefSeq; WP_000210375.1; NC_010658.1.
DR AlphaFoldDB; B2U1I5; -.
DR STRING; 344609.SbBS512_E1702; -.
DR MEROPS; M03.005; -.
DR KEGG; sbc:SbBS512_E1702; -.
DR HOGENOM; CLU_001805_4_0_6; -.
DR OMA; FDHIWGG; -.
DR Proteomes; UP000001030; 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:ACD08988.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000001030};
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; 77587 MW; 1CBA615B708F9AA0 CRC64;
MTTMNPFLVQ STLPYLAPHF DQIANHHYRP AFDEGMQQKR AEIAAIALNP QTPDFNNTIL
ALEQSGELLT RVTSVFFAMT AAHTNDELQR LDEQFSAELA ELANDIYLNG ELFARVDAVW
QRRESLGLDS ESIRLVEVIH QRFVLAGAKL AQADKAKLKV LNTEAATLTS QFNQRLLAAN
KSGGLVVNDI AQLAGMSEQE IALAAEAARE KGLDNKWLIP LLNTTQQPAL AEMRDRATRE
KLFIAGWTRA EKNDANDTRA IIQRLVEIRA QQAKLLDFPH 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 GNSEDLERLY
RQWRGKAPQI MPMLQHRGLN I
//