DACA_HAEIN
ID DACA_HAEIN Reviewed; 393 AA.
AC P44466;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=D-alanyl-D-alanine carboxypeptidase DacA;
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=HI_0029;
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: Removes C-terminal D-alanyl residues from sugar-peptide cell
CC wall precursors. {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: Cell inner membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Note=N-terminal lies in the periplasmic
CC space. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S11 family. {ECO:0000305}.
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DR EMBL; L42023; AAC21707.1; -; Genomic_DNA.
DR PIR; I64043; I64043.
DR RefSeq; NP_438202.1; NC_000907.1.
DR RefSeq; WP_005693881.1; NC_000907.1.
DR PDB; 3A3J; X-ray; 2.15 A; A=30-373.
DR PDBsum; 3A3J; -.
DR AlphaFoldDB; P44466; -.
DR SMR; P44466; -.
DR STRING; 71421.HI_0029; -.
DR EnsemblBacteria; AAC21707; AAC21707; HI_0029.
DR KEGG; hin:HI_0029; -.
DR PATRIC; fig|71421.8.peg.29; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_8_1_6; -.
DR OMA; QNTHFQT; -.
DR PhylomeDB; P44466; -.
DR BioCyc; HINF71421:G1GJ1-29-MON; -.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; P44466; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
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 3D-structure; Carboxypeptidase; Cell inner membrane; Cell membrane;
KW Cell shape; Cell wall biogenesis/degradation; Hydrolase; Membrane;
KW Peptidoglycan synthesis; Protease; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..393
FT /note="D-alanyl-D-alanine carboxypeptidase DacA"
FT /id="PRO_0000027232"
FT ACT_SITE 65
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 68
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 128
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:3A3J"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:3A3J"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:3A3J"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:3A3J"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:3A3J"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:3A3J"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:3A3J"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:3A3J"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:3A3J"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:3A3J"
FT HELIX 130..141
FT /evidence="ECO:0007829|PDB:3A3J"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:3A3J"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:3A3J"
FT HELIX 180..193
FT /evidence="ECO:0007829|PDB:3A3J"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:3A3J"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:3A3J"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:3A3J"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:3A3J"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:3A3J"
FT STRAND 225..235
FT /evidence="ECO:0007829|PDB:3A3J"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:3A3J"
FT STRAND 239..247
FT /evidence="ECO:0007829|PDB:3A3J"
FT STRAND 253..263
FT /evidence="ECO:0007829|PDB:3A3J"
FT HELIX 264..281
FT /evidence="ECO:0007829|PDB:3A3J"
FT STRAND 282..288
FT /evidence="ECO:0007829|PDB:3A3J"
FT STRAND 293..310
FT /evidence="ECO:0007829|PDB:3A3J"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:3A3J"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:3A3J"
FT STRAND 328..340
FT /evidence="ECO:0007829|PDB:3A3J"
FT STRAND 347..355
FT /evidence="ECO:0007829|PDB:3A3J"
FT STRAND 358..367
FT /evidence="ECO:0007829|PDB:3A3J"
SQ SEQUENCE 393 AA; 43414 MW; 31DF0C563A833B7C CRC64;
MLKRTTKIAF LSSFVALSAF SVSAEDMQFG VTPPQITAQT YVLMDYNSGA ILTALNPDQR
QYPASLTKMM TSYVVGVALK QGKIHNTDMV TIGESAWGRN FPDSSKMFLD LNTQVSVADL
NRGVIVVSGN DATVALAEHI SGNVPNFVET MNKYVQQFGL KNTNFTTPHG LDDPNQYSSA
RDMAIIGAHI IRDLPEEYKI YSEKNFTFNK IKQANRNGLL WDKTINVDGM KTGHTSQAGY
NLVASATTSN NMRLISVVMG VPTYKGREVE SKKLLQWGFA NFETFKTLEA GKEISEQRVY
YGDKNSVKLG ALMDHFITIP KGKQSEVKAR YELADKNLQA PLVKGQVIGK VVYQLDGKDI
ASANLQVMND VGEAGIFGKL WDWLVLTVKG LFS
