(data stored in SCRATCH zone)

SWISSPROT: DACA_BACSU

ID   DACA_BACSU              Reviewed;         443 AA.
AC   P08750;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 3.
DT   11-DEC-2019, entry version 151.
DE   RecName: Full=D-alanyl-D-alanine carboxypeptidase DacA;
DE            Short=CPase;
DE            Short=DD-carboxypeptidase;
DE            Short=DD-peptidase;
DE            EC=3.4.16.4;
DE   AltName: Full=Penicillin-binding protein 5;
DE            Short=PBP-5;
DE   Flags: Precursor;
GN   Name=dacA; OrderedLocusNames=BSU00100;
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;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
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   PROTEIN SEQUENCE OF 32-102.
RX   PubMed=6768745;
RA   Waxman D.J., Strominger J.L.;
RT   "Sequence of active site peptides from the penicillin-sensitive D-alanine
RT   carboxypeptidase of Bacillus subtilis. Mechanism of penicillin action and
RT   sequence homology to beta-lactamases.";
RL   J. Biol. Chem. 255:3964-3976(1980).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 103-443.
RX   PubMed=3087956; DOI=10.1128/jb.167.1.257-264.1986;
RA   Todd J.A., Roberts A.N., Johnstone K., Piggot P.J., Winter G., Ellar D.J.;
RT   "Reduced heat resistance of mutant spores after cloning and mutagenesis of
RT   the Bacillus subtilis gene encoding penicillin-binding protein 5.";
RL   J. Bacteriol. 167:257-264(1986).
RN   [5]
RP   PROTEIN SEQUENCE OF 414-443.
RX   PubMed=6780559;
RA   Waxman D.J., Strominger J.L.;
RT   "Primary structure of the COOH-terminal membranous segment of a penicillin-
RT   sensitive enzyme purified from two Bacilli.";
RL   J. Biol. Chem. 256:2067-2077(1981).
RN   [6]
RP   ACTIVE SITE SER-67.
RX   PubMed=111240; DOI=10.1073/pnas.76.6.2730;
RA   Yocum R.R., Waxman D.J., Rasmussen J.R., Strominger J.L.;
RT   "Mechanism of penicillin action: penicillin and substrate bind covalently
RT   to the same active site serine in two bacterial D-alanine
RT   carboxypeptidases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 76:2730-2734(1979).
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, cell wall.
CC   -!- SIMILARITY: Belongs to the peptidase S11 family. {ECO:0000305}.
DR   EMBL; D26185; BAA05246.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11786.1; -; Genomic_DNA.
DR   EMBL; M13766; AAA22375.1; -; Genomic_DNA.
DR   PIR; S66040; S66040.
DR   RefSeq; NP_387891.1; NC_000964.3.
DR   RefSeq; WP_009966224.1; NZ_JNCM01000024.1.
DR   SMR; P08750; -.
DR   STRING; 224308.BSU00100; -.
DR   ChEMBL; CHEMBL3112381; -.
DR   MEROPS; S11.001; -.
DR   jPOST; P08750; -.
DR   PaxDb; P08750; -.
DR   PRIDE; P08750; -.
DR   EnsemblBacteria; CAB11786; CAB11786; BSU00100.
DR   GeneID; 940000; -.
DR   KEGG; bsu:BSU00100; -.
DR   PATRIC; fig|224308.179.peg.10; -.
DR   eggNOG; COG1686; LUCA.
DR   HOGENOM; HOG000086625; -.
DR   InParanoid; P08750; -.
DR   KO; K07258; -.
DR   OMA; QNTHFQT; -.
DR   PhylomeDB; P08750; -.
DR   BioCyc; BSUB:BSU00100-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   PRO; PR:P08750; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; ISA:CACAO.
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: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   1: Evidence at protein level;
DR   PRODOM; P08750.
DR   SWISS-2DPAGE; P08750.
KW   Carboxypeptidase; Cell shape; Cell wall; Cell wall biogenesis/degradation;
KW   Direct protein sequencing; Hydrolase; Peptidoglycan synthesis; Protease;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000269|PubMed:6768745"
FT   CHAIN           32..443
FT                   /note="D-alanyl-D-alanine carboxypeptidase DacA"
FT                   /id="PRO_0000027228"
FT   ACT_SITE        67
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000269|PubMed:111240"
FT   ACT_SITE        70
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000250"
FT   BINDING         258
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        100
FT                   /note="E -> Q (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        227
FT                   /note="E -> Q (in Ref. 4; AAA22375)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   443 AA;  48636 MW;  DA6C5B0307D7C117 CRC64;
     MNIKKCKQLL MSLVVLTLAV TCLAPMSKAK AASDPIDINA SAAIMIEASS GKILYSKNAD
     KRLPIASMTK MMTEYLLLEA IDQGKVKWDQ TYTPDDYVYE ISQDNSLSNV PLRKDGKYTV
     KELYQATAIY SANAAAIAIA EIVAGSETKF VEKMNAKAKE LGLTDYKFVN ATGLENKDLH
     GHQPEGTSVN EESEVSAKDM AVLADHLITD YPEILETSSI AKTKFREGTD DEMDMPNWNF
     MLKGLVSEYK KATVDGLKTG STDSAGSCFT GTAERNGMRV ITVVLNAKGN LHTGRFDETK
     KMFDYAFDNF SMKEIYAEGD QVKGHKTISV DKGKEKEVGI VTNKAFSLPV KNGEEKNYKA
     KVTLNKDNLT APVKKGTKVG KLTAEYTGDE KDYGFLNSDL AGVDLVTKEN VEKANWFVLT
     MRSIGGFFAG IWGSIVDTVT GWF
//

If you have problems or comments...

PBIL Back to PBIL home page