ID   K4L328_SIMAS            Unreviewed;       614 AA.
AC   K4L328;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Dipeptidyl carboxydipeptidase family protein {ECO:0000313|EMBL:AFV00608.1};
GN   OrderedLocusNames=M5M_17395 {ECO:0000313|EMBL:AFV00608.1};
OS   Simiduia agarivorans (strain DSM 21679 / JCM 13881 / BCRC 17597 / SA1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Simiduia.
OX   NCBI_TaxID=1117647 {ECO:0000313|EMBL:AFV00608.1, ECO:0000313|Proteomes:UP000000466};
RN   [1] {ECO:0000313|EMBL:AFV00608.1, ECO:0000313|Proteomes:UP000000466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21679 / JCM 13881 / BCRC 17597 / SA1
RC   {ECO:0000313|Proteomes:UP000000466};
RX   PubMed=23405302; DOI=10.1128/genomeA.00039-12;
RA   Lin S.Y., Shieh W.Y., Chen J.S., Tang S.L.;
RT   "Complete genome sequence of Simiduia agarivorans SA1(T), a marine
RT   bacterium able to degrade a variety of polysaccharides.";
RL   Genome Announc. 1:E00039-E00039(2013).
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DR   EMBL; CP003746; AFV00608.1; -; Genomic_DNA.
DR   RefSeq; WP_015048760.1; NZ_ATUQ01000001.1.
DR   AlphaFoldDB; K4L328; -.
DR   STRING; 1117647.M5M_17395; -.
DR   KEGG; saga:M5M_17395; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_014364_3_0_6; -.
DR   OrthoDB; 5241329at2; -.
DR   Proteomes; UP000000466; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd06461; M2_ACE; 1.
DR   Gene3D; 1.10.1370.30; -; 2.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   PANTHER; PTHR10514:SF27; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   Pfam; PF01401; Peptidase_M2; 1.
DR   PRINTS; PR00791; PEPDIPTASEA.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000466};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
SQ   SEQUENCE   614 AA;  68705 MW;  C3E99441D4733E1E CRC64;
     MRTPHKLSVL ALAVATGLLV GCQPEGKEKA TVAQAEAAKV YDQAAADAFL EEAEAALKDT
     AEYASRASWL AATYINGDSQ FVEARASKEY TLQVVKYAMQ VKNWDGAQVD PVTRRKLDAL
     RLGLSFPSPA DEKLAGELAD IGSKMQGMYG AGKYCRESGE CLDLIQMSNI LAEGKDPALM
     MEVWTGWRSV SPPMRPLYQR QVEIANAGAQ DLGFENLSVL WRSNYDMAPD AFAADVDKQW
     GKVKPLYDAL HCHVRAKLNE AYGDDVVPAT GKIPAHMLGN MWAQTWGNVY DKVKPANSQK
     SYDLTKLIEK SGMNEIGMVR TAEAFFSSLG FAPLPDSFWE TSQFVKPRDR DVVCHASAWN
     MDSKDDLRIK MCIQKNGEDF QTVHHELGHN YYQRAYNQQP FLFQGSANDG FHEALGDTVA
     LSITPSYLVS LGMLKEEPPV SEDLGYLMQM ALDKIAFLPF GLLVDKWRWQ VFNGEIKPED
     YNKGWWSLRE QYQGITPPVA RSEADFDPGA KYHIPGNTPY TRYFLAFIQQ FQFHRSLCET
     AGYEGPLHRC SIYNNKAAGD KLQAMMAMGT SQPWQNAMQA LTGQPELDAS AIVDYFAPLK
     VWLDEQNKDR QCGW
//