ID   B8E4Z4_SHEB2            Unreviewed;       734 AA.
AC   B8E4Z4;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Peptidyl-dipeptidase Dcp {ECO:0000313|EMBL:ACK46229.1};
DE            EC=3.4.15.5 {ECO:0000313|EMBL:ACK46229.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Sbal223_1724 {ECO:0000313|EMBL:ACK46229.1};
OS   Shewanella baltica (strain OS223).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=407976 {ECO:0000313|EMBL:ACK46229.1, ECO:0000313|Proteomes:UP000002507};
RN   [1] {ECO:0000313|Proteomes:UP000002507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS223 {ECO:0000313|Proteomes:UP000002507};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ovchinnikova G., Brettar I., Rodrigues J., Konstantinidis K.,
RA   Tiedje J.;
RT   "Complete sequence of chromosome of Shewanella baltica OS223.";
RL   Submitted (DEC-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; CP001252; ACK46229.1; -; Genomic_DNA.
DR   RefSeq; WP_012587400.1; NC_011663.1.
DR   AlphaFoldDB; B8E4Z4; -.
DR   KEGG; sbp:Sbal223_1724; -.
DR   HOGENOM; CLU_001805_4_0_6; -.
DR   Proteomes; UP000002507; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:ACK46229.1};
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   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..734
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002867757"
FT   DOMAIN          282..730
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   734 AA;  81837 MW;  C2FA7D71DC87DCF5 CRC64;
     MKGLTLKPQA RTAKLTLSAI ALALTLGACS TQQPEASVQA NAAPNAVSAQ IISQNATNPF
     FKPYDTFMEI PAFDKIKPEH FLPAFKAGVA QQHEQIQAIV DNKAKPTFAN TIEAMEFSGD
     LVTRVSNVFF NLTGADTTPA LQALSKEVSP MLSSAEDDIL LNDKLFQKVK AVHDAKDSLK
     LSTAQAKLLE DTYKSFTRGG ANLSEQDKTK LRALNEEIGK LNLAFGDNLL AETNAFELVV
     DNKADLAGLP ADVIATAFET AKKRGHEGKW VFTTSRPSIT PFLTYADNRQ LREKLYKGYI
     ERGNNNNAND NKIILAKIAA LRAERAQLMG YKTHADFVLE ERTAKTPENV YGLLNKVWPA
     ALAQAKTEVA DMQAMIDAQG GKFKLQAWDW DYYADKIRVA KYSFNEQQTR PYFSLDSTLK
     GVFYTANRLY GLTFKERTDL PKYNAEVRTW EVYDKDGKLM AIFMGDYFTR DSKRGGAWMN
     SFRKQYNMNG VDSKPIIVNV LNYPRPAGNE PALLTFDEAS TLFHEFGHAL HGMLSNVEYR
     SQGGTAVPRD YVEFPSQVNE NWMTQPEVLA QFAKHYKTGE VIPQELVKKI QAASKFNQGF
     ATVEYMAATK LDLDWHTLTD TTPKDAAKFE ADSLAAMGLI EEISPRYRST YFSHIFAGGY
     SAGYYSYLWS DILGADAFEA FKENGIFDKA TADSFRNNIL SKGGSDDPML MYKNFRGKEA
     GIEPLLRSRG LLAE
//