ID   CBXPD_MYCS2             Reviewed;         460 AA.
AC   A0R596; I7GA32;
DT   03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   03-JUL-2019, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Carboxypeptidase DacB {ECO:0000305};
DE            EC=3.4.16.- {ECO:0000250|UniProtKB:O06380};
DE   Flags: Precursor;
GN   Name=dacB {ECO:0000303|PubMed:30914728};
GN   OrderedLocusNames=MSMEG_6113 {ECO:0000312|EMBL:ABK75663.1},
GN   MSMEI_5954 {ECO:0000312|EMBL:AFP42387.1};
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=30914728; DOI=10.1038/s41598-019-41001-x;
RA   Ealand C.S., Asmal R., Mashigo L., Campbell L., Kana B.D.;
RT   "Characterization of putative DD-carboxypeptidase-encoding genes in
RT   Mycobacterium smegmatis.";
RL   Sci. Rep. 9:5194-5194(2019).
CC   -!- FUNCTION: Carboxypeptidase that cleaves terminal D-alanine from
CC       peptidoglycan in the mycobacterial cell wall. May cleave L-Lys-D-Ala
CC       and/or D-Ala-D-Ala peptide bonds. Exerts important effects on
CC       mycobacterial cell morphology and cell division.
CC       {ECO:0000250|UniProtKB:O06380}.
CC   -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted.
CC       {ECO:0000269|PubMed:30914728}.
CC   -!- SIMILARITY: Belongs to the peptidase S13 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK75663.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AFP42387.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000480; ABK75663.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP001663; AFP42387.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_029104179.1; NZ_SIJM01000043.1.
DR   RefSeq; YP_890334.1; NC_008596.1.
DR   AlphaFoldDB; A0R596; -.
DR   SMR; A0R596; -.
DR   STRING; 246196.MSMEI_5954; -.
DR   MEROPS; S13.004; -.
DR   PRIDE; A0R596; -.
DR   EnsemblBacteria; ABK75663; ABK75663; MSMEG_6113.
DR   EnsemblBacteria; AFP42387; AFP42387; MSMEI_5954.
DR   GeneID; 66737397; -.
DR   KEGG; msg:MSMEI_5954; -.
DR   KEGG; msm:MSMEG_6113; -.
DR   PATRIC; fig|246196.19.peg.5952; -.
DR   eggNOG; COG2027; Bacteria.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; -; 2.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR000667; Peptidase_S13.
DR   PANTHER; PTHR30023; PTHR30023; 2.
DR   Pfam; PF02113; Peptidase_S13; 1.
DR   PRINTS; PR00922; DADACBPTASE3.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   TIGRFAMs; TIGR00666; PBP4; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Cell wall biogenesis/degradation; Hydrolase; Protease;
KW   Reference proteome; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..460
FT                   /note="Carboxypeptidase DacB"
FT                   /id="PRO_5010266702"
FT   REGION          39..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        113
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P39844"
FT   ACT_SITE        116
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P39844"
FT   ACT_SITE        294
FT                   /evidence="ECO:0000250|UniProtKB:P39844"
SQ   SEQUENCE   460 AA;  46911 MW;  1A52A0CA482AB938 CRC64;
     MRPTRWRRST HVAVGVAVLA LVVAVVAAAA LFTGKHSDAA EAVPPAPPPA TADPGVVPVD
     LSAPTPTRRG LATALAAALA NPDLGLITGR ITDADTGAEL WEQGARVPMQ PASVNKVLTT
     AAALLTLDRD ARLTTTVVAA DDQPGLVVLR GGGDTTLSAA PKGTDTWYKG AARISDLADQ
     VRARGIRVTR VRVDTSAYSG PTMAPGWDPA DIDGGDIAPM ESVMLDGGRT QPTTVESRRS
     KSPALDAGKA LAAALGVEPE SVTLMPSGMR GGTTIAEVQS APLIERLRQM MNESDNVMAE
     SIAREVAEAL GRPQSFEGAV GAVLTQLRSV GIDTSGAKLV DSSGLSVDNR LTALTLDEVV
     NAAAGHTQPA LRPLVDLLPI AGGSGTLSNR YLDTDAGRAA AGWLRAKTGS LTGTNALAGI
     VTDRSGRVLT FALISNNAGP TGRTAIDALA AVLRSCGCGA