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Database: UniProt
Entry: L0J2N2_9MYCO
LinkDB: L0J2N2_9MYCO
Original site: L0J2N2_9MYCO 
ID   L0J2N2_9MYCO            Unreviewed;       211 AA.
AC   L0J2N2;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:AGB25113.1};
DE   Flags: Precursor;
GN   ORFNames=Mycsm_04894 {ECO:0000313|EMBL:AGB25113.1};
OS   Mycobacterium sp. JS623.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB25113.1, ECO:0000313|Proteomes:UP000010844};
RN   [1] {ECO:0000313|Proteomes:UP000010844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS623 {ECO:0000313|Proteomes:UP000010844};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A., Rutledge P.,
RA   Paulsen I., Coleman N., Woyke T.;
RT   "Complete sequence of chromosome of Mycobacterium smegmatis JS623.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP003078; AGB25113.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0J2N2; -.
DR   STRING; 212767.Mycsm_04894; -.
DR   KEGG; msa:Mycsm_04894; -.
DR   PATRIC; fig|710686.3.peg.4927; -.
DR   HOGENOM; CLU_104140_0_0_11; -.
DR   OrthoDB; 3293184at2; -.
DR   Proteomes; UP000010844; Chromosome.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd14846; Peptidase_M15_like; 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:AGB25113.1};
KW   Hydrolase {ECO:0000313|EMBL:AGB25113.1};
KW   Protease {ECO:0000313|EMBL:AGB25113.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..41
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           42..211
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003943965"
FT   DOMAIN          91..180
FT                   /note="Peptidase M15B"
FT                   /evidence="ECO:0000259|Pfam:PF02557"
SQ   SEQUENCE   211 AA;  22161 MW;  A7B5869B6195E817 CRC64;
     MSSLPRACVS ARRHAAFNVH FAHARGLLSA TALLISGCAA AVPIEPIATT EPTAAPAPLT
     IGPAATDTYG GWIPDGQTLS PFDTSNPAVG QLDPALLKAV QDAADAAKQQ GVDLRINSGW
     RSTGFQQRLF DNAVRGYGSV DIARQFVASP DVSKHVVGQA VDIAPVDADN WLIRNGAQFG
     LCQIYANELW HFELAVDPQG NCPPLRPNAA G
//
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