ID   LDC_BACSU               Reviewed;         319 AA.
AC   O34851;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Probable murein peptide carboxypeptidase;
DE            EC=3.4.16.-;
DE   AltName: Full=LD-carboxypeptidase;
GN   Name=ykfA; OrderedLocusNames=BSU12970;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Devine K.M.;
RT   "Sequence of the Bacillus subtilis genome between xlyA and ykoR.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION TO N-TERMINUS.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [4]
RP   INDUCTION.
RX   PubMed=15101989; DOI=10.1111/j.1365-2958.2004.04023.x;
RA   Hamon M.A., Stanley N.R., Britton R.A., Grossman A.D., Lazazzera B.A.;
RT   "Identification of AbrB-regulated genes involved in biofilm formation by
RT   Bacillus subtilis.";
RL   Mol. Microbiol. 52:847-860(2004).
CC   -!- FUNCTION: May be involved in the degradation of peptidoglycan by
CC       catalyzing the cleavage of the terminal D-alanine residue from
CC       cytoplasmic murein peptides. {ECO:0000250}.
CC   -!- PATHWAY: Cell wall degradation; peptidoglycan degradation.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: Repressed by AbrB, a transcription factor that negatively
CC       controls biofilm formation. {ECO:0000269|PubMed:15101989}.
CC   -!- SIMILARITY: Belongs to the peptidase S66 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA05577.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AJ002571; CAA05577.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL009126; CAB13154.2; -; Genomic_DNA.
DR   PIR; G69855; G69855.
DR   RefSeq; NP_389180.2; NC_000964.3.
DR   RefSeq; WP_009967072.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O34851; -.
DR   SMR; O34851; -.
DR   STRING; 224308.BSU12970; -.
DR   MEROPS; S66.001; -.
DR   PaxDb; O34851; -.
DR   PRIDE; O34851; -.
DR   EnsemblBacteria; CAB13154; CAB13154; BSU_12970.
DR   GeneID; 938175; -.
DR   KEGG; bsu:BSU12970; -.
DR   PATRIC; fig|224308.179.peg.1409; -.
DR   eggNOG; COG1619; Bacteria.
DR   InParanoid; O34851; -.
DR   OMA; MLTQWRL; -.
DR   PhylomeDB; O34851; -.
DR   BioCyc; BSUB:BSU12970-MON; -.
DR   UniPathway; UPA00549; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10740; -; 1.
DR   Gene3D; 3.50.30.60; -; 1.
DR   InterPro; IPR027461; Carboxypeptidase_A_C_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR027478; LdcA_N.
DR   InterPro; IPR040449; Peptidase_S66_N.
DR   InterPro; IPR040921; Peptidase_S66C.
DR   InterPro; IPR003507; S66_fam.
DR   PANTHER; PTHR30237; PTHR30237; 1.
DR   Pfam; PF02016; Peptidase_S66; 1.
DR   Pfam; PF17676; Peptidase_S66C; 1.
DR   PIRSF; PIRSF028757; LD-carboxypeptidase; 1.
DR   SUPFAM; SSF141986; SSF141986; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase; Cell wall biogenesis/degradation; Cytoplasm; Hydrolase;
KW   Protease; Reference proteome; Serine protease.
FT   CHAIN           1..319
FT                   /note="Probable murein peptide carboxypeptidase"
FT                   /id="PRO_0000172841"
FT   ACT_SITE        116
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        214
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        284
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   319 AA;  34596 MW;  1E328AA2BC5077EE CRC64;
     MKGVFSLNYK PKALNKGDTV GVIAPASPPD PKKLDTALLF LEELGLQVKL GKALKNQHGY
     LAGQDDERLA DLHEMFRDDE VKAVLCACGG FGTGRIAAGI DFSLIRKHPK IFWGYSDITF
     LHTAIHQNTG LVTFHGPMLS TDIGLDDVHP LTKASYKQLF QETEFTYTEE LSPLTELVPG
     KAEGELVGGN LSLLTSTLGT PFEIDTRGKL LFIEDIDEEP YQIDRMLNQL KMGGKLTDAA
     GILVCDFHNC VPVKREKSLS LEQVLEDYII SAGRPALRGF KIGHCSPSIA VPIGAKAAMN
     TAEKTAVIEA GVSEGALKT