DACB_HAEIN
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 03-AUG-2022, entry version 136.
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; Proteobacteria; 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}.
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DR EMBL; L42023; AAC22975.1; -; Genomic_DNA.
DR PIR; A64117; A64117.
DR RefSeq; NP_439482.1; NC_000907.1.
DR RefSeq; WP_005694445.1; 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 PRIDE; P45161; -.
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 OMA; DGTMRKR; -.
DR PhylomeDB; P45161; -.
DR BioCyc; HINF71421:G1GJ1-1355-MON; -.
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; 3.40.710.10; -; 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; 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
