ID   DACF_BACSU              Reviewed;         389 AA.
AC   P38422;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=D-alanyl-D-alanine carboxypeptidase DacF;
DE            Short=DD-carboxypeptidase;
DE            Short=DD-peptidase;
DE            EC=3.4.16.4;
DE   AltName: Full=Penicillin-binding protein DacF;
DE            Short=PBP;
DE   Flags: Precursor;
GN   Name=dacF; OrderedLocusNames=BSU23480;
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 / MB24;
RX   PubMed=1629150; DOI=10.1128/jb.174.15.4885-4892.1992;
RA   Wu J.-J., Schuch R., Piggot P.J.;
RT   "Characterization of a Bacillus subtilis sporulation operon that includes
RT   genes for an RNA polymerase sigma factor and for a putative DD-
RT   carboxypeptidase.";
RL   J. Bacteriol. 174:4885-4892(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
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).
CC   -!- FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell
CC       wall precursors.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC         transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC         substituents of D-alanine.; EC=3.4.16.4;
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the forespore.
CC   -!- SIMILARITY: Belongs to the peptidase S11 family. {ECO:0000305}.
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DR   EMBL; M85047; AAA22704.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12652.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14280.1; -; Genomic_DNA.
DR   PIR; B42708; B42708.
DR   RefSeq; NP_390229.1; NC_000964.3.
DR   RefSeq; WP_004398637.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P38422; -.
DR   SMR; P38422; -.
DR   STRING; 224308.BSU23480; -.
DR   MEROPS; S11.005; -.
DR   PaxDb; P38422; -.
DR   PRIDE; P38422; -.
DR   EnsemblBacteria; CAB14280; CAB14280; BSU_23480.
DR   GeneID; 938732; -.
DR   KEGG; bsu:BSU23480; -.
DR   PATRIC; fig|224308.179.peg.2558; -.
DR   eggNOG; COG1686; Bacteria.
DR   InParanoid; P38422; -.
DR   OMA; TNEAKYC; -.
DR   PhylomeDB; P38422; -.
DR   BioCyc; BSUB:BSU23480-MON; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.410.10; -; 1.
DR   Gene3D; 3.40.710.10; -; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR015956; Peniciliin-bd_prot_C_sf.
DR   InterPro; IPR018044; Peptidase_S11.
DR   InterPro; IPR012907; Peptidase_S11_C.
DR   InterPro; IPR037167; Peptidase_S11_C_sf.
DR   InterPro; IPR001967; Peptidase_S11_N.
DR   Pfam; PF07943; PBP5_C; 1.
DR   Pfam; PF00768; Peptidase_S11; 1.
DR   PRINTS; PR00725; DADACBPTASE1.
DR   SMART; SM00936; PBP5_C; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   SUPFAM; SSF69189; SSF69189; 1.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase; Cell shape; Cell wall biogenesis/degradation; Hydrolase;
KW   Peptidoglycan synthesis; Protease; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..389
FT                   /note="D-alanyl-D-alanine carboxypeptidase DacF"
FT                   /id="PRO_0000027230"
FT   ACT_SITE        64
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        67
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        124
FT                   /evidence="ECO:0000250"
FT   BINDING         230
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        376
FT                   /note="T -> S (in Ref. 1; AAA22704)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   389 AA;  43297 MW;  8252AD2FF91E42AE CRC64;
     MKRLLSTLLI GIMLLTFAPS AFAKQDGKRT SELAHEAKSA VLIERDTGKV LYNKNSNERL
     APASMTKIMT MLLIMEALDK GKIKMSDKVR TSEHAASMGG SQIFLEPGEE MTVKEMLKGI
     AIASGNDASV AMAEFISGSE EEFVKKMNKK AKELGLKNTS FKNPTGLTEE GHYSSAYDMA
     IMAKELLKYE SITKFTGTYE DYLRENTDKK FWLVNTNRLI KFYPGVDGVK TGYTGEAKYC
     LTASAKKGNM RAIAVVFGAS TPKERNAQVT KMLDFAFSQY ETHPLYKRNQ TVAKVKVKKG
     KQKFIELTTS EPISILTKKG EDMNDVKKEI KMKDNISAPI QKGQELGTLV LKKDGEVLAE
     SPVAAKEDMK KAGFITFLKR TMGDWTKFK