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 03-AUG-2022, entry version 161.
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; DOI=10.1016/s0021-9258(19)85620-x;
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; DOI=10.1016/s0021-9258(19)69916-3;
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).
RN [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=20713508; DOI=10.1101/gad.1945010;
RA Lopez D., Kolter R.;
RT "Functional microdomains in bacterial membranes.";
RL Genes Dev. 24:1893-1902(2010).
RN [8]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=22882210; DOI=10.1111/j.1365-2958.2012.08205.x;
RA Yepes A., Schneider J., Mielich B., Koch G., Garcia-Betancur J.C.,
RA Ramamurthi K.S., Vlamakis H., Lopez D.;
RT "The biofilm formation defect of a Bacillus subtilis flotillin-defective
RT mutant involves the protease FtsH.";
RL Mol. Microbiol. 86:457-471(2012).
RN [9]
RP INTERACTION WITH FLOT, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=23651456; DOI=10.1111/mmi.12252;
RA Bach J.N., Bramkamp M.;
RT "Flotillins functionally organize the bacterial membrane.";
RL Mol. Microbiol. 88:1205-1217(2013).
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. Cell membrane
CC {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210}. Membrane
CC raft {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210,
CC ECO:0000269|PubMed:23651456}. Note=Present in detergent-resistant
CC membrane (DRM) fractions that may be equivalent to eukaryotic membrane
CC rafts; these rafts include proteins involved in signaling, molecule
CC trafficking and protein secretion. {ECO:0000269|PubMed:20713508,
CC ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23651456}.
CC -!- SIMILARITY: Belongs to the peptidase S11 family. {ECO:0000305}.
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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 AlphaFoldDB; P08750; -.
DR SMR; P08750; -.
DR STRING; 224308.BSU00100; -.
DR BindingDB; P08750; -.
DR ChEMBL; CHEMBL3112381; -.
DR MEROPS; S11.001; -.
DR jPOST; P08750; -.
DR PaxDb; P08750; -.
DR PRIDE; P08750; -.
DR EnsemblBacteria; CAB11786; CAB11786; BSU_00100.
DR GeneID; 940000; -.
DR KEGG; bsu:BSU00100; -.
DR PATRIC; fig|224308.179.peg.10; -.
DR eggNOG; COG1686; Bacteria.
DR InParanoid; P08750; -.
DR OMA; QNTHFQT; -.
DR PhylomeDB; P08750; -.
DR BioCyc; BSUB:BSU00100-MON; -.
DR UniPathway; UPA00219; -.
DR PRO; PR:P08750; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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: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 1: Evidence at protein level;
KW Carboxypeptidase; Cell membrane; Cell shape; Cell wall;
KW Cell wall biogenesis/degradation; Direct protein sequencing; Hydrolase;
KW Membrane; Peptidoglycan synthesis; Protease; Reference proteome; Secreted;
KW 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 /ligand="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
