Reviewed, UniProtKB/Swiss-Prot P08750 (DACA_BACSU)

Names and origin

Protein names

Recommended name:
    D-alanyl-D-alanine carboxypeptidase dacA
      Short name=DD-carboxypeptidase
      Short name=DD-peptidase
      Short name=CPase
    EC=3.4.16.4
Alternative name(s):
    Penicillin-binding protein 5
      Short name=PBP-5

Gene names

Name:	dacA
Ordered Locus Names:	BSU00100

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	443 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
Catalytic activity	Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular location	Secreted › cell wall.
Sequence similarities	Belongs to the peptidase S11 family.

Ontologies

Keywords
Biological process	Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cell wall Secreted
Domain	Signal
Molecular function	Carboxypeptidase Hydrolase Protease
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	serine-type D-Ala-D-Ala carboxypeptidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 31	31	Ref.3
	Chain	32 – 443	412	D-alanyl-D-alanine carboxypeptidase dacA		PRO_0000027228
Sites
	Active site	67	1	Acyl-ester intermediate Ref.6
	Active site	70	1	Proton acceptor By similarity
	Active site	131	1	By similarity
	Binding site	258	1	Substrate By similarity
Experimental info
	Sequence conflict	100	1	E → Q AA sequence Ref.3
	Sequence conflict	227	1	E → Q in AAA22375. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P08750-1 [UniParc]. Last modified October 1, 1994. Version 3. Checksum: DA6C5B0307D7C117	FASTA	443	48,636
	10 20 30 40 50 60 MNIKKCKQLL MSLVVLTLAV TCLAPMSKAK AASDPIDINA SAAIMIEASS GKILYSKNAD 70 80 90 100 110 120 KRLPIASMTK MMTEYLLLEA IDQGKVKWDQ TYTPDDYVYE ISQDNSLSNV PLRKDGKYTV 130 140 150 160 170 180 KELYQATAIY SANAAAIAIA EIVAGSETKF VEKMNAKAKE LGLTDYKFVN ATGLENKDLH 190 200 210 220 230 240 GHQPEGTSVN EESEVSAKDM AVLADHLITD YPEILETSSI AKTKFREGTD DEMDMPNWNF 250 260 270 280 290 300 MLKGLVSEYK KATVDGLKTG STDSAGSCFT GTAERNGMRV ITVVLNAKGN LHTGRFDETK 310 320 330 340 350 360 KMFDYAFDNF SMKEIYAEGD QVKGHKTISV DKGKEKEVGI VTNKAFSLPV KNGEEKNYKA 370 380 390 400 410 420 KVTLNKDNLT APVKKGTKVG KLTAEYTGDE KDYGFLNSDL AGVDLVTKEN VEKANWFVLT 430 440 MRSIGGFFAG IWGSIVDTVT GWF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin." Ogasawara N., Nakai S., Yoshikawa H. DNA Res. 1:1-14(1994) [PubMed: 7584024] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Sequence of active site peptides from the penicillin-sensitive D-alanine carboxypeptidase of Bacillus subtilis. Mechanism of penicillin action and sequence homology to beta-lactamases." Waxman D.J., Strominger J.L. J. Biol. Chem. 255:3964-3976(1980) [PubMed: 6768745] [Abstract] Cited for: PROTEIN SEQUENCE OF 32-102.
[4]	"Reduced heat resistance of mutant spores after cloning and mutagenesis of the Bacillus subtilis gene encoding penicillin-binding protein 5." Todd J.A., Roberts A.N., Johnstone K., Piggot P.J., Winter G., Ellar D.J. J. Bacteriol. 167:257-264(1986) [PubMed: 3087956] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 103-443.
[5]	"Primary structure of the COOH-terminal membranous segment of a penicillin-sensitive enzyme purified from two Bacilli." Waxman D.J., Strominger J.L. J. Biol. Chem. 256:2067-2077(1981) [PubMed: 6780559] [Abstract] Cited for: PROTEIN SEQUENCE OF 414-443.
[6]	"Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases." Yocum R.R., Waxman D.J., Rasmussen J.R., Strominger J.L. Proc. Natl. Acad. Sci. U.S.A. 76:2730-2734(1979) [PubMed: 111240] [Abstract] Cited for: ACTIVE SITE SER-67.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D26185 Genomic DNA. Translation: BAA05246.1. AL009126 Genomic DNA. Translation: CAB11786.1. M13766 Genomic DNA. Translation: AAA22375.1.
PIR	S66040.
RefSeq	NP_387891.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	S11.001.
Genome annotation databases
GeneID	940000.
GenomeReviews	Gene locus BSU00100 in contig AL009126_GR.
KEGG	bsu:BSU00100.
NMPDR	fig|224308.1.peg.10.
Organism-specific databases
SubtiList	BG10074. dacA. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P08750.
OMA	YSNASAE
Enzyme and pathway databases
BRENDA	3.4.16.4. 150.
Family and domain databases
InterPro	IPR012338. B-lactamase-typ_transpept_fold. IPR015956. Peniciliin-bd_prot-assoc. IPR001967. Peptidase_S11. IPR012907. Peptidase_S11_C. IPR018044. Peptidase_S11_cons-region. [Graphical view]
Gene3D	G3DSA:2.60.410.10. Peptidase_S11_C. 1 hit.
Pfam	PF07943. PBP5_C. 1 hit. PF00768. Peptidase_S11. 1 hit. [Graphical view]
PRINTS	PR00725. DADACBPTASE1.
ProtoNet	Search...

Entry information

Entry name

DACA_BACSU

Accession

Primary (citable) accession number: P08750

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	October 1, 1994
Last modified:	November 24, 2009
This is version 91 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)