ID   A3QF30_SHELP            Unreviewed;       720 AA.
AC   A3QF30;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   SubName: Full=Peptidyl-dipeptidase Dcp {ECO:0000313|EMBL:ABO24078.1};
DE            EC=3.4.15.5 {ECO:0000313|EMBL:ABO24078.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Shew_2212 {ECO:0000313|EMBL:ABO24078.1};
OS   Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=323850 {ECO:0000313|EMBL:ABO24078.1, ECO:0000313|Proteomes:UP000001558};
RN   [1] {ECO:0000313|EMBL:ABO24078.1, ECO:0000313|Proteomes:UP000001558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1088 / PV-4 {ECO:0000313|Proteomes:UP000001558};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA   Fredrickson J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella loihica PV-4.";
RL   Submitted (MAR-2007) 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; CP000606; ABO24078.1; -; Genomic_DNA.
DR   RefSeq; WP_011866010.1; NC_009092.1.
DR   AlphaFoldDB; A3QF30; -.
DR   KEGG; slo:Shew_2212; -.
DR   eggNOG; COG0339; Bacteria.
DR   HOGENOM; CLU_001805_4_0_6; -.
DR   OrthoDB; 9773538at2; -.
DR   Proteomes; UP000001558; 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:ABO24078.1};
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:UP000001558};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          274..717
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   720 AA;  79722 MW;  5636A24370AD9FA1 CRC64;
     MRKSILTTAI LAGLYLTGCT PASQEAINTE VASTEAAKPA VQASEGQINA SNVLLKKSVL
     QYQAPEFDKI TFDDYAPAFT QGIIEHDKEI QAIIDNQAAA DFDNTIVAME KSGSLLTRVA
     KTFFNLASVN SNSQVQTLEA ELAPKLSAHW DNIFLNPELF ARVESVYKSR DSLSAEDKHL
     VEYYYLAFER AGAKLSDADK EKMRDLNGQL ASLTTEFSKN VLDSFKNEVI IVKDKAELDG
     LSDAEIATLA QAAKDAGKEG YLITLVNTTR QPILSSLNNR ELREKVWKTS ANRAMALNGP
     NIVKQSHLHA EKAALLGYDS WAAYTVADQM AKTPTAVYEI LDDLAPKAVA KAKLEAADIQ
     AQIKASGQDF ELAPWDWAYY SEKVRKAKYD LDQSQVTPYF EFNRVLNDGL FFAMEKLYGI
     TVKPRKDLPV WNPDVLAYEI FNKDKSSIGI FYLDPYAREG KNGGAWMDEF VTQSGLLGTK
     PVVYNALNIP KPASGPTLMT YDEVSTMFHE FGHAVHGLFS QVKYPSVAGT ATPRDFVEFP
     SQANEDWSID PEVLANYAKH YQTGEPIPAE LLKKVLAASK FGQGFDTTEY LAAAILDMEW
     HSIGVDAKID DVAKFEQQAL AKHGIDFAPI PPRYKSAYFS HAFAGGYSAG YYAYLWTEVF
     AADAFDFMSH NGGLSLENGN KFRDNVLSKG NSEDLMQDYI KFTGRKPTVD ALLKHRGLTE
//