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Database: UniProt
Entry: K4KJK4_SIMAS
LinkDB: K4KJK4_SIMAS
Original site: K4KJK4_SIMAS 
ID   K4KJK4_SIMAS            Unreviewed;       346 AA.
AC   K4KJK4;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Peptidase M15B and M15C, D,D-carboxypeptidase VanY/endolysin {ECO:0000313|EMBL:AFU98178.1};
GN   OrderedLocusNames=M5M_04855 {ECO:0000313|EMBL:AFU98178.1};
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:AFU98178.1, ECO:0000313|Proteomes:UP000000466};
RN   [1] {ECO:0000313|EMBL:AFU98178.1, 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; AFU98178.1; -; Genomic_DNA.
DR   RefSeq; WP_015046351.1; NZ_ATUQ01000006.1.
DR   AlphaFoldDB; K4KJK4; -.
DR   STRING; 1117647.M5M_04855; -.
DR   KEGG; saga:M5M_04855; -.
DR   eggNOG; COG1876; Bacteria.
DR   HOGENOM; CLU_068880_0_0_6; -.
DR   OrthoDB; 9786184at2; -.
DR   Proteomes; UP000000466; Chromosome.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd14814; Peptidase_M15; 1.
DR   Gene3D; 3.30.1380.10; -; 1.
DR   InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR   InterPro; IPR003709; Pept_M15B.
DR   PANTHER; PTHR34385; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR34385:SF1; PEPTIDOGLYCAN L-ALANYL-D-GLUTAMATE ENDOPEPTIDASE CWLK; 1.
DR   Pfam; PF02557; VanY; 1.
DR   SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:AFU98178.1};
KW   Hydrolase {ECO:0000313|EMBL:AFU98178.1};
KW   Protease {ECO:0000313|EMBL:AFU98178.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000466}.
FT   DOMAIN          241..344
FT                   /note="Peptidase M15B"
FT                   /evidence="ECO:0000259|Pfam:PF02557"
SQ   SEQUENCE   346 AA;  38752 MW;  25C6D3C227219373 CRC64;
     MKRRELLTGL FATSGFALSN GLLWKYAQDT FSPNTAQDPL VTGNISDSES VRQLAAVDVI
     RDAGPAATTD RVVQKTPDPA FAELKASPPK AAVVKQPEPQ PEVAANDQAD RILDKVRNFE
     QEFADDIYLN QDERILMHSV LQRLSRAEAL IGHGNYNICS FDYLLKIADR YSQVGSFSKP
     ELAFIERLFF EDATNYGFLG DRVSTELTAT IADRDVLKIP YSGQYVFRGE SEAYYQKIKK
     DIGDSIILTS GIRSNVKQMH LFLAKASVSN YNLSKASRSL APPGHSYHGI GDFDVGKVGW
     GIANFSDKFA ETDEFKRMQD LGYVQIRYTE DNRLGVRFEP WHIKVV
//
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