DACC_BACSU
ID DACC_BACSU Reviewed; 491 AA.
AC P39844;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=D-alanyl-D-alanine carboxypeptidase DacC;
DE Short=DD-carboxypeptidase;
DE Short=DD-peptidase;
DE EC=3.4.16.4;
DE AltName: Full=Penicillin-binding protein 4a;
DE Short=PBP-4a;
DE Flags: Precursor;
GN Name=dacC; Synonyms=pbp; OrderedLocusNames=BSU18350;
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=7711903; DOI=10.1099/13500872-141-3-645;
RA Tognoni A., Franchi E., Magistrelli C., Colombo E., Cosmina P., Grandi G.;
RT "A putative new peptide synthase operon in Bacillus subtilis: partial
RT characterization.";
RL Microbiology 141:645-648(1995).
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 30-34, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC STRAIN=168 / PS832;
RX PubMed=9733705; DOI=10.1128/jb.180.18.4967-4973.1998;
RA Pedersen L.B., Murray T., Popham D.L., Setlow P.;
RT "Characterization of dacC, which encodes a new low-molecular-weight
RT penicillin-binding protein in Bacillus subtilis.";
RL J. Bacteriol. 180:4967-4973(1998).
RN [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=168 / BGSC1A1;
RX PubMed=11160090; DOI=10.1128/jb.183.5.1595-1599.2001;
RA Duez C., Vanhove M., Gallet X., Bouillenne F., Docquier J.-D., Brans A.,
RA Frere J.-M.;
RT "Purification and characterization of PBP4a, a new low-molecular-weight
RT penicillin-binding protein from Bacillus subtilis.";
RL J. Bacteriol. 183:1595-1599(2001).
RN [5]
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 [6]
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 [7] {ECO:0007744|PDB:1W5D, ECO:0007744|PDB:2J9P}
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 30-491 OF APOENZYME AND IN COMPLEX
RP WITH SUBSTRATE ANALOG, REACTION MECHANISM, AND ACTIVE SITE.
RX PubMed=17582436; DOI=10.1016/j.jmb.2007.05.071;
RA Sauvage E., Duez C., Herman R., Kerff F., Petrella S., Anderson J.W.,
RA Adediran S.A., Pratt R.F., Frere J.-M., Charlier P.;
RT "Crystal structure of the Bacillus subtilis penicillin-binding protein 4a,
RT and its complex with a peptidoglycan mimetic peptide.";
RL J. Mol. Biol. 371:528-539(2007).
CC -!- FUNCTION: Catalyzes DD-carboxypeptidase and transpeptidation reactions.
CC {ECO:0000269|PubMed:11160090}.
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 -!- ACTIVITY REGULATION: Inhibited by cephaloridine.
CC {ECO:0000269|PubMed:11160090}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=400 uM for N(alpha)-acetyl-L-Lys-D-Ala-D-thiolactate
CC {ECO:0000269|PubMed:11160090};
CC KM=470 uM for benzoyl-Gly-thiogylcolate
CC {ECO:0000269|PubMed:11160090};
CC KM=380 uM for benzoyl-D-Ala-thiogylcolate
CC {ECO:0000269|PubMed:11160090};
CC pH dependence:
CC Optimum pH is 12. {ECO:0000269|PubMed:11160090};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22882210,
CC ECO:0000305|PubMed:9733705}. Membrane raft
CC {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210}. Note=May be
CC anchored in the membrane via a C-terminal amphipathic alpha helix.
CC Present in detergent-resistant membrane (DRM) fractions that may be
CC equivalent to eukaryotic membrane rafts; these rafts include proteins
CC involved in signaling, molecule trafficking and protein secretion
CC (PubMed:20713508, PubMed:22882210). {ECO:0000269|PubMed:20713508,
CC ECO:0000269|PubMed:22882210}.
CC -!- DEVELOPMENTAL STAGE: Expression starts at the end of the exponential
CC phase and peaks two hours into sporulation. There is no enzyme activity
CC in spores. {ECO:0000269|PubMed:9733705}.
CC -!- INDUCTION: Expression is sigma H-dependent.
CC {ECO:0000269|PubMed:9733705}.
CC -!- SIMILARITY: Belongs to the peptidase S13 family. {ECO:0000305}.
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DR EMBL; Z34883; CAA84366.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13718.1; -; Genomic_DNA.
DR PIR; I40455; I40455.
DR RefSeq; NP_389717.1; NC_000964.3.
DR RefSeq; WP_004399303.1; NZ_JNCM01000036.1.
DR PDB; 1W5D; X-ray; 2.10 A; A=30-491.
DR PDB; 2J9P; X-ray; 2.80 A; A/B=30-491.
DR PDBsum; 1W5D; -.
DR PDBsum; 2J9P; -.
DR AlphaFoldDB; P39844; -.
DR SMR; P39844; -.
DR STRING; 224308.BSU18350; -.
DR MEROPS; S13.002; -.
DR PaxDb; P39844; -.
DR PRIDE; P39844; -.
DR EnsemblBacteria; CAB13718; CAB13718; BSU_18350.
DR GeneID; 939990; -.
DR KEGG; bsu:BSU18350; -.
DR PATRIC; fig|224308.179.peg.2002; -.
DR eggNOG; COG2027; Bacteria.
DR InParanoid; P39844; -.
DR OMA; DGTMRKR; -.
DR PhylomeDB; P39844; -.
DR BioCyc; BSUB:BSU18350-MON; -.
DR BRENDA; 3.4.16.4; 658.
DR SABIO-RK; P39844; -.
DR EvolutionaryTrace; P39844; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; -; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000667; Peptidase_S13.
DR PANTHER; PTHR30023; PTHR30023; 1.
DR Pfam; PF02113; Peptidase_S13; 1.
DR PRINTS; PR00922; DADACBPTASE3.
DR SUPFAM; SSF56601; SSF56601; 1.
DR TIGRFAMs; TIGR00666; PBP4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Direct protein sequencing; Hydrolase;
KW Membrane; Peptidoglycan synthesis; Reference proteome; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:9733705"
FT CHAIN 30..491
FT /note="D-alanyl-D-alanine carboxypeptidase DacC"
FT /id="PRO_0000027243"
FT ACT_SITE 81
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000305|PubMed:17582436"
FT ACT_SITE 84
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:17582436"
FT ACT_SITE 328
FT /evidence="ECO:0000305|PubMed:17582436"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:17582436"
FT BINDING 328..330
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:17582436"
FT BINDING 381
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:17582436"
FT BINDING 441..445
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:17582436"
FT HELIX 35..46
FT /evidence="ECO:0007829|PDB:1W5D"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1W5D"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:1W5D"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1W5D"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:1W5D"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:1W5D"
FT HELIX 84..95
FT /evidence="ECO:0007829|PDB:1W5D"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:1W5D"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:1W5D"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:1W5D"
FT HELIX 132..144
FT /evidence="ECO:0007829|PDB:1W5D"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1W5D"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:1W5D"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:1W5D"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:1W5D"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:1W5D"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:1W5D"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:1W5D"
FT STRAND 222..233
FT /evidence="ECO:0007829|PDB:1W5D"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:1W5D"
FT STRAND 249..261
FT /evidence="ECO:0007829|PDB:1W5D"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:1W5D"
FT HELIX 274..288
FT /evidence="ECO:0007829|PDB:1W5D"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:1W5D"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:1W5D"
FT STRAND 306..313
FT /evidence="ECO:0007829|PDB:1W5D"
FT HELIX 317..327
FT /evidence="ECO:0007829|PDB:1W5D"
FT HELIX 330..344
FT /evidence="ECO:0007829|PDB:1W5D"
FT HELIX 350..360
FT /evidence="ECO:0007829|PDB:1W5D"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:1W5D"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:1W5D"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:1W5D"
FT HELIX 387..397
FT /evidence="ECO:0007829|PDB:1W5D"
FT HELIX 403..409
FT /evidence="ECO:0007829|PDB:1W5D"
FT HELIX 418..421
FT /evidence="ECO:0007829|PDB:1W5D"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:1W5D"
FT STRAND 425..428
FT /evidence="ECO:0007829|PDB:2J9P"
FT TURN 432..436
FT /evidence="ECO:0007829|PDB:1W5D"
FT STRAND 437..444
FT /evidence="ECO:0007829|PDB:1W5D"
FT STRAND 447..455
FT /evidence="ECO:0007829|PDB:1W5D"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:1W5D"
FT STRAND 461..470
FT /evidence="ECO:0007829|PDB:1W5D"
FT HELIX 474..476
FT /evidence="ECO:0007829|PDB:1W5D"
FT HELIX 477..489
FT /evidence="ECO:0007829|PDB:1W5D"
SQ SEQUENCE 491 AA; 52891 MW; E442E5A227B7D080 CRC64;
MKKSIKLYVA VLLLFVVASV PYMHQAALAA EKQDALSGQI DKILADHPAL EGAMAGITVR
SAETGAVLYE HSGDTRMRPA SSLKLLTAAA ALSVLGENYS FTTEVRTDGT LKGKKLNGNL
YLKGKGDPTL LPSDFDKMAE ILKHSGVKVI KGNLIGDDTW HDDMRLSPDM PWSDEYTYYG
APISALTASP NEDYDAGTVI VEVTPNQKEG EEPAVSVSPK TDYITIKNDA KTTAAGSEKD
LTIEREHGTN TITIEGSVPV DANKTKEWIS VWEPAGYALD LFKQSLKKQG ITVKGDIKTG
EAPSSSDVLL SHRSMPLSKL FVPFMKLSNN GHAEVLVKEM GKVKKGEGSW EKGLEVLNST
LPEFGVDSKS LVLRDGSGIS HIDAVSSDQL SQLLYDIQDQ SWFSAYLNSL PVAGNPDRMV
GGTLRNRMKG TPAQGKVRAK TGSLSTVSSL SGYAETKSGK KLVFSILLNG LIDEEDGKDI
EDQIAVILAN Q
