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Database: UniProt
Entry: A9DI16_9GAMM
LinkDB: A9DI16_9GAMM
Original site: A9DI16_9GAMM 
ID   A9DI16_9GAMM            Unreviewed;       258 AA.
AC   A9DI16;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   03-MAY-2023, entry version 56.
DE   SubName: Full=Peptidyl-dipeptidase {ECO:0000313|EMBL:EDP99133.1};
DE   Flags: Fragment;
GN   ORFNames=KT99_11008 {ECO:0000313|EMBL:EDP99133.1};
OS   Shewanella benthica KT99.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=314608 {ECO:0000313|EMBL:EDP99133.1, ECO:0000313|Proteomes:UP000005839};
RN   [1] {ECO:0000313|EMBL:EDP99133.1, ECO:0000313|Proteomes:UP000005839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT99 {ECO:0000313|EMBL:EDP99133.1,
RC   ECO:0000313|Proteomes:UP000005839};
RA   Yayanos A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (OCT-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|RuleBase:RU003435}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDP99133.1}.
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DR   EMBL; ABIC01000051; EDP99133.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9DI16; -.
DR   Proteomes; UP000005839; Unassembled WGS sequence.
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   Gene3D; 1.10.1370.40; -; 2.
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   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          1..254
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EDP99133.1"
SQ   SEQUENCE   258 AA;  29093 MW;  D24CDA58755E012E CRC64;
     AWMSSYRQQY KMNGVDSKPI IVNVLNYPRP SAGEPSLLTF DEASTLFHEF GHALHGMLSD
     VQYRSQAGTS VPRDYVEFPS QVMENWMTQP EVLAQFAKHY KTGEVIPQEL VKKIQAASKF
     NQGFATVEYM AATKLDLDWH TVTDFTPKDA AKFEAESLNK MGLINEIAPR YRSTYFAHIF
     SGGYSAGYYS YLWSDILGAD AFEAFKENGI FDQTTAEAFR NNILSQGGSE DPMLLYKQFR
     GKEAGIDPLL RSRGLLAK
//
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