ID DACB_HAEIN Reviewed; 479 AA. AC P45161; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 143. DE RecName: Full=D-alanyl-D-alanine carboxypeptidase DacB; DE Short=DD-carboxypeptidase; DE Short=DD-peptidase; DE EC=3.4.16.4; DE AltName: Full=D-alanyl-D-alanine endopeptidase; DE Short=DD-endopeptidase; DE EC=3.4.21.-; DE AltName: Full=Penicillin-binding protein 4; DE Short=PBP-4; DE Flags: Precursor; GN Name=dacB; OrderedLocusNames=HI_1330; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Not involved in transpeptidation but exclusively catalyzes a CC DD-carboxypeptidase and DD-endopeptidase reaction. {ECO:0000250}. 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: Periplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the peptidase S13 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L42023; AAC22975.1; -; Genomic_DNA. DR PIR; A64117; A64117. DR RefSeq; NP_439482.1; NC_000907.1. DR PDB; 3A3D; X-ray; 1.60 A; A/B=28-479. DR PDB; 3A3E; X-ray; 2.40 A; A/B=28-479. DR PDB; 3A3F; X-ray; 2.10 A; A/B=28-479. DR PDB; 3A3I; X-ray; 2.00 A; A/B=28-479. DR PDBsum; 3A3D; -. DR PDBsum; 3A3E; -. DR PDBsum; 3A3F; -. DR PDBsum; 3A3I; -. DR AlphaFoldDB; P45161; -. DR SMR; P45161; -. DR STRING; 71421.HI_1330; -. DR MEROPS; S13.001; -. DR EnsemblBacteria; AAC22975; AAC22975; HI_1330. DR KEGG; hin:HI_1330; -. DR PATRIC; fig|71421.8.peg.1383; -. DR eggNOG; COG2027; Bacteria. DR HOGENOM; CLU_017692_1_1_6; -. DR OrthoDB; 9802627at2; -. DR PhylomeDB; P45161; -. DR BioCyc; HINF71421:G1GJ1-1355-MONOMER; -. DR UniPathway; UPA00219; -. DR EvolutionaryTrace; P45161; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; 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-UniPathway. 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 GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR Gene3D; 3.50.80.20; D-Ala-D-Ala carboxypeptidase C, peptidase S13; 1. DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR000667; Peptidase_S13. DR NCBIfam; TIGR00666; PBP4; 1. DR PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1. DR PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1. DR Pfam; PF02113; Peptidase_S13; 1. DR PRINTS; PR00922; DADACBPTASE3. DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic resistance; Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Hydrolase; Peptidoglycan synthesis; KW Periplasm; Reference proteome; Signal. FT SIGNAL 1..26 FT /evidence="ECO:0000255" FT CHAIN 27..479 FT /note="D-alanyl-D-alanine carboxypeptidase DacB" FT /id="PRO_0000027242" FT ACT_SITE 69 FT /note="Acyl-ester intermediate" FT /evidence="ECO:0000250|UniProtKB:P39844" FT ACT_SITE 72 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P39844" FT ACT_SITE 310 FT /evidence="ECO:0000250|UniProtKB:P39844" FT BINDING 420 FT /ligand="substrate" FT /evidence="ECO:0000250" FT HELIX 30..34 FT /evidence="ECO:0007829|PDB:3A3D" FT STRAND 42..49 FT /evidence="ECO:0007829|PDB:3A3D" FT TURN 50..53 FT /evidence="ECO:0007829|PDB:3A3D" FT STRAND 54..60 FT /evidence="ECO:0007829|PDB:3A3D" FT HELIX 68..71 FT /evidence="ECO:0007829|PDB:3A3D" FT HELIX 72..82 FT /evidence="ECO:0007829|PDB:3A3D" FT STRAND 90..97 FT /evidence="ECO:0007829|PDB:3A3D" FT STRAND 108..111 FT /evidence="ECO:0007829|PDB:3A3D" FT HELIX 120..132 FT /evidence="ECO:0007829|PDB:3A3D" FT STRAND 142..145 FT /evidence="ECO:0007829|PDB:3A3D" FT HELIX 160..162 FT /evidence="ECO:0007829|PDB:3A3D" FT HELIX 166..168 FT /evidence="ECO:0007829|PDB:3A3D" FT HELIX 177..179 FT /evidence="ECO:0007829|PDB:3A3D" FT STRAND 180..186 FT /evidence="ECO:0007829|PDB:3A3D" FT STRAND 196..198 FT /evidence="ECO:0007829|PDB:3A3D" FT STRAND 206..208 FT /evidence="ECO:0007829|PDB:3A3D" FT STRAND 212..214 FT /evidence="ECO:0007829|PDB:3A3D" FT TURN 216..218 FT /evidence="ECO:0007829|PDB:3A3D" FT HELIX 219..221 FT /evidence="ECO:0007829|PDB:3A3D" FT STRAND 224..229 FT /evidence="ECO:0007829|PDB:3A3D" FT TURN 230..232 FT /evidence="ECO:0007829|PDB:3A3D" FT STRAND 233..241 FT /evidence="ECO:0007829|PDB:3A3D" FT STRAND 247..252 FT /evidence="ECO:0007829|PDB:3A3D" FT HELIX 256..270 FT /evidence="ECO:0007829|PDB:3A3D" FT STRAND 289..295 FT /evidence="ECO:0007829|PDB:3A3D" FT HELIX 299..309 FT /evidence="ECO:0007829|PDB:3A3D" FT HELIX 312..327 FT /evidence="ECO:0007829|PDB:3A3D" FT HELIX 333..346 FT /evidence="ECO:0007829|PDB:3A3D" FT STRAND 359..361 FT /evidence="ECO:0007829|PDB:3A3D" FT HELIX 370..382 FT /evidence="ECO:0007829|PDB:3A3D" FT HELIX 384..387 FT /evidence="ECO:0007829|PDB:3A3D" FT HELIX 390..392 FT /evidence="ECO:0007829|PDB:3A3D" FT TURN 396..398 FT /evidence="ECO:0007829|PDB:3A3D" FT HELIX 400..402 FT /evidence="ECO:0007829|PDB:3A3D" FT HELIX 406..408 FT /evidence="ECO:0007829|PDB:3A3D" FT TURN 411..416 FT /evidence="ECO:0007829|PDB:3A3D" FT STRAND 418..424 FT /evidence="ECO:0007829|PDB:3A3D" FT STRAND 427..435 FT /evidence="ECO:0007829|PDB:3A3D" FT STRAND 441..450 FT /evidence="ECO:0007829|PDB:3A3D" FT HELIX 463..478 FT /evidence="ECO:0007829|PDB:3A3D" SQ SEQUENCE 479 AA; 52686 MW; 632868C61206CB48 CRC64; MKKLSSISTA LGSFLLSVSF SLPTFANINV SDLTQKLPEG SNVGFIAKNI NQNQIIADYN GSTFMLSAST QKVFTAVAAK LALDDQFQFE TALLSNGKIQ NGNLDGNLIV RFTGDPDLTR GQLYSLLAEL KKQGIKKING DLVLDTSVFS SHDRGLGWIW NDLTMCFNSP PAAANIDNNC FYAELDANKN PGEIVKINVP AQFPIQVFGQ VYVADSNEAP YCQLDVVVHD NNRYQVKGCL ARQYKPFGLS FAVQNTDAYA AEIIQRQLRQ LGIEFNGKVL LPQKPQQGQL LAKHLSKPLP DLLKKMMKKS DNQIADSLFR AVAFNYYKRP ASFQLGTLAV KSILQKQGIR FGNSILADGS GLSRHNLVAP KTMLSVLEYI AKNEDKLHLM ETFPIAGVDG TISGRGGLIS PPLVKNVIAK TGSLKGVYNL AGFMTNARGE KVAFVQFING YSTGDLESKT KRAPLVQFER NLYNELYKY //