LDC_PSEAE
ID LDC_PSEAE Reviewed; 307 AA.
AC Q9HTZ1;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Murein tetrapeptide carboxypeptidase;
DE EC=3.4.17.13;
DE AltName: Full=LD-carboxypeptidase;
GN OrderedLocusNames=PA5198;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-115 AND
RP ALA-285, CATALYTIC ACTIVITY, IDENTIFICATION AS A SERINE PEPTIDASE, ACTIVE
RP SITE, SUBUNIT, AND MUTAGENESIS OF SER-115; GLU-217 AND HIS-285.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=16162494; DOI=10.1074/jbc.m506328200;
RA Korza H.J., Bochtler M.;
RT "Pseudomonas aeruginosa LD-carboxypeptidase, a serine peptidase with a Ser-
RT His-Glu triad and a nucleophilic elbow.";
RL J. Biol. Chem. 280:40802-40812(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS).
RG Midwest center for structural genomics (MCSG);
RT "X-ray crystal structure of hypothetical protein PA5198 at 1.1 A
RT resolution.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Releases the terminal D-alanine residue from the cytoplasmic
CC disaccharide-tetrapeptide GlcNAc-MurNAc-L-Ala-gamma-D-Glu-meso-Dap-D-
CC Ala, which is a murein turnover product. Probably also act on free
CC tetrapetide. May be involved in murein recycling.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-alanyl-D-
CC glutamyl-6-carboxy-L-lysyl-D-alanine = D-alanine + N-acetyl-D-
CC glucosaminyl-N-acetylmuramoyl-L-alanyl-D-glutamyl-6-carboxy-L-lysyl;
CC Xref=Rhea:RHEA:48688, ChEBI:CHEBI:15377, ChEBI:CHEBI:57416,
CC ChEBI:CHEBI:90762, ChEBI:CHEBI:90763; EC=3.4.17.13;
CC Evidence={ECO:0000269|PubMed:16162494};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:16162494}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S66 family. {ECO:0000305}.
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DR EMBL; AE004091; AAG08583.1; -; Genomic_DNA.
DR PIR; E82997; E82997.
DR RefSeq; NP_253885.1; NC_002516.2.
DR RefSeq; WP_003100070.1; NZ_QZGE01000002.1.
DR PDB; 1ZL0; X-ray; 1.10 A; A/B=1-307.
DR PDB; 1ZRS; X-ray; 1.50 A; A/B=1-307.
DR PDB; 2AUM; X-ray; 2.40 A; A/B=1-307.
DR PDB; 2AUN; X-ray; 2.40 A; A/B=1-307.
DR PDBsum; 1ZL0; -.
DR PDBsum; 1ZRS; -.
DR PDBsum; 2AUM; -.
DR PDBsum; 2AUN; -.
DR AlphaFoldDB; Q9HTZ1; -.
DR SMR; Q9HTZ1; -.
DR STRING; 287.DR97_2567; -.
DR MEROPS; S66.001; -.
DR PaxDb; Q9HTZ1; -.
DR PRIDE; Q9HTZ1; -.
DR DNASU; 880289; -.
DR EnsemblBacteria; AAG08583; AAG08583; PA5198.
DR GeneID; 880289; -.
DR KEGG; pae:PA5198; -.
DR PATRIC; fig|208964.12.peg.5448; -.
DR PseudoCAP; PA5198; -.
DR HOGENOM; CLU_034346_3_1_6; -.
DR InParanoid; Q9HTZ1; -.
DR OMA; GFIFGQC; -.
DR PhylomeDB; Q9HTZ1; -.
DR BioCyc; MetaCyc:MON-20218; -.
DR BioCyc; PAER208964:G1FZ6-5317-MON; -.
DR BRENDA; 3.4.17.13; 5087.
DR UniPathway; UPA00544; -.
DR EvolutionaryTrace; Q9HTZ1; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0106415; F:muramoyltetrapeptide carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008236; F:serine-type peptidase activity; 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:0009254; P:peptidoglycan turnover; 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; 3.40.50.10740; -; 1.
DR Gene3D; 3.50.30.60; -; 1.
DR InterPro; IPR027461; Carboxypeptidase_A_C_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR027478; LdcA_N.
DR InterPro; IPR040449; Peptidase_S66_N.
DR InterPro; IPR040921; Peptidase_S66C.
DR InterPro; IPR003507; S66_fam.
DR PANTHER; PTHR30237; PTHR30237; 1.
DR Pfam; PF02016; Peptidase_S66; 1.
DR Pfam; PF17676; Peptidase_S66C; 1.
DR PIRSF; PIRSF028757; LD-carboxypeptidase; 1.
DR SUPFAM; SSF141986; SSF141986; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carboxypeptidase; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Hydrolase;
KW Peptidoglycan synthesis; Protease; Reference proteome; Serine protease.
FT CHAIN 1..307
FT /note="Murein tetrapeptide carboxypeptidase"
FT /id="PRO_0000388973"
FT ACT_SITE 115
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:16162494"
FT ACT_SITE 217
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:16162494"
FT ACT_SITE 285
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:16162494"
FT MUTAGEN 115
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16162494"
FT MUTAGEN 217
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16162494"
FT MUTAGEN 285
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16162494"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:1ZL0"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1ZRS"
FT HELIX 29..41
FT /evidence="ECO:0007829|PDB:1ZL0"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1ZL0"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:1ZL0"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1ZL0"
FT HELIX 63..75
FT /evidence="ECO:0007829|PDB:1ZL0"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:1ZL0"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:1ZL0"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:1ZL0"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:1ZL0"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:1ZL0"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:1ZL0"
FT HELIX 118..126
FT /evidence="ECO:0007829|PDB:1ZL0"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1ZL0"
FT HELIX 137..141
FT /evidence="ECO:0007829|PDB:1ZL0"
FT HELIX 148..165
FT /evidence="ECO:0007829|PDB:1ZL0"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1ZL0"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:1ZL0"
FT STRAND 184..192
FT /evidence="ECO:0007829|PDB:1ZL0"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:1ZL0"
FT TURN 198..201
FT /evidence="ECO:0007829|PDB:1ZL0"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:1ZL0"
FT HELIX 223..236
FT /evidence="ECO:0007829|PDB:1ZL0"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:1ZL0"
FT STRAND 243..251
FT /evidence="ECO:0007829|PDB:1ZL0"
FT HELIX 262..272
FT /evidence="ECO:0007829|PDB:1ZL0"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:1ZL0"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:1ZL0"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:1ZL0"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:1ZL0"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:1ZL0"
SQ SEQUENCE 307 AA; 33288 MW; 0E6BA75C30DC8C9B CRC64;
MTSRPSSDQT WQPIDGRVAL IAPASAIATD VLEATLRQLE VHGVDYHLGR HVEARYRYLA
GTVEQRLEDL HNAFDMPDIT AVWCLRGGYG CGQLLPGLDW GRLQAASPRP LIGFSDISVL
LSAFHRHGLP AIHGPVATGL GLSPLSAPRE QQERLASLAS VSRLLAGIDH ELPVQHLGGH
KQRVEGALIG GNLTALACMA GTLGGLHAPA GSILVLEDVG EPYYRLERSL WQLLESIDAR
QLGAICLGSF TDCPRKEVAH SLERIFGEYA AAIEVPLYHH LPSGHGAQNR AWPYGKTAVL
EGNRLRW
