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Protein

Murein tetrapeptide carboxypeptidase

Gene

PA5198

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Releases the terminal D-alanine residue from the cytoplasmic disaccharide-tetrapeptide GlcNAc-MurNAc-L-Ala-gamma-D-Glu-meso-Dap-D-Ala, which is a murein turnover product. Probably also act on free tetrapetide. May be involved in murein recycling.

Catalytic activityi

GlcNAc-MurNAc-L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanine + H2O = GlcNAc-MurNAc-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate + D-alanine.1 Publication

Pathwayi: peptidoglycan recycling

This protein is involved in the pathway peptidoglycan recycling, which is part of Cell wall biogenesis.
View all proteins of this organism that are known to be involved in the pathway peptidoglycan recycling and in Cell wall biogenesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei115 – 1151Nucleophile1 Publication
Active sitei217 – 2171Charge relay system1 Publication
Active sitei285 – 2851Charge relay system1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Protease, Serine protease

Keywords - Biological processi

Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

BRENDAi3.4.17.13. 5087.
UniPathwayiUPA00544.

Protein family/group databases

MEROPSiS66.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Murein tetrapeptide carboxypeptidase (EC:3.4.17.13)
Alternative name(s):
LD-carboxypeptidase
Gene namesi
Ordered Locus Names:PA5198
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA5198.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi115 – 1151S → A: Loss of activity. 1 Publication
Mutagenesisi217 – 2171E → A: Loss of activity. 1 Publication
Mutagenesisi285 – 2851H → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 307307Murein tetrapeptide carboxypeptidasePRO_0000388973Add
BLAST

Proteomic databases

PaxDbiQ9HTZ1.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi208964.PA5198.

Structurei

Secondary structure

1
307
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 216Combined sources
Beta strandi23 – 253Combined sources
Helixi29 – 4113Combined sources
Beta strandi46 – 483Combined sources
Turni50 – 534Combined sources
Beta strandi59 – 613Combined sources
Helixi63 – 7513Combined sources
Beta strandi79 – 857Combined sources
Helixi91 – 944Combined sources
Turni95 – 973Combined sources
Helixi100 – 1056Combined sources
Beta strandi111 – 1133Combined sources
Helixi115 – 1173Combined sources
Helixi118 – 1269Combined sources
Beta strandi131 – 1333Combined sources
Helixi137 – 1415Combined sources
Helixi148 – 16518Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi175 – 1795Combined sources
Beta strandi184 – 1929Combined sources
Helixi193 – 1975Combined sources
Turni198 – 2014Combined sources
Beta strandi213 – 2208Combined sources
Helixi223 – 23614Combined sources
Helixi239 – 2413Combined sources
Beta strandi243 – 2519Combined sources
Helixi262 – 27211Combined sources
Beta strandi277 – 2793Combined sources
Beta strandi284 – 2874Combined sources
Beta strandi292 – 2943Combined sources
Beta strandi297 – 3015Combined sources
Beta strandi304 – 3074Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZL0X-ray1.10A/B1-307[»]
1ZRSX-ray1.50A/B1-307[»]
2AUMX-ray2.40A/B1-307[»]
2AUNX-ray2.40A/B1-307[»]
ProteinModelPortaliQ9HTZ1.
SMRiQ9HTZ1. Positions 3-307.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HTZ1.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S66 family.Curated

Phylogenomic databases

eggNOGiENOG4107WMG. Bacteria.
COG1619. LUCA.
HOGENOMiHOG000025480.
InParanoidiQ9HTZ1.
KOiK01297.
OMAiPVIMNHE.
OrthoDBiEOG6JTC7M.
PhylomeDBiQ9HTZ1.

Family and domain databases

Gene3Di3.40.50.10740. 1 hit.
3.50.30.60. 1 hit.
InterProiIPR027461. Carboxypeptidase_A_C.
IPR029062. Class_I_gatase-like.
IPR027478. LdcA_N_dom.
IPR003507. S66_fam.
[Graphical view]
PfamiPF02016. Peptidase_S66. 1 hit.
[Graphical view]
PIRSFiPIRSF028757. LD-carboxypeptidase. 1 hit.
SUPFAMiSSF141986. SSF141986. 1 hit.
SSF52317. SSF52317. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9HTZ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSRPSSDQT WQPIDGRVAL IAPASAIATD VLEATLRQLE VHGVDYHLGR
60 70 80 90 100
HVEARYRYLA GTVEQRLEDL HNAFDMPDIT AVWCLRGGYG CGQLLPGLDW
110 120 130 140 150
GRLQAASPRP LIGFSDISVL LSAFHRHGLP AIHGPVATGL GLSPLSAPRE
160 170 180 190 200
QQERLASLAS VSRLLAGIDH ELPVQHLGGH KQRVEGALIG GNLTALACMA
210 220 230 240 250
GTLGGLHAPA GSILVLEDVG EPYYRLERSL WQLLESIDAR QLGAICLGSF
260 270 280 290 300
TDCPRKEVAH SLERIFGEYA AAIEVPLYHH LPSGHGAQNR AWPYGKTAVL

EGNRLRW
Length:307
Mass (Da):33,288
Last modified:March 1, 2001 - v1
Checksum:i0E6BA75C30DC8C9B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG08583.1.
PIRiE82997.
RefSeqiNP_253885.1. NC_002516.2.
WP_003100070.1. NZ_ASJY01000813.1.

Genome annotation databases

EnsemblBacteriaiAAG08583; AAG08583; PA5198.
GeneIDi880289.
KEGGipae:PA5198.
PATRICi19845243. VBIPseAer58763_5448.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG08583.1.
PIRiE82997.
RefSeqiNP_253885.1. NC_002516.2.
WP_003100070.1. NZ_ASJY01000813.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZL0X-ray1.10A/B1-307[»]
1ZRSX-ray1.50A/B1-307[»]
2AUMX-ray2.40A/B1-307[»]
2AUNX-ray2.40A/B1-307[»]
ProteinModelPortaliQ9HTZ1.
SMRiQ9HTZ1. Positions 3-307.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA5198.

Protein family/group databases

MEROPSiS66.001.

Proteomic databases

PaxDbiQ9HTZ1.

Protocols and materials databases

DNASUi880289.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG08583; AAG08583; PA5198.
GeneIDi880289.
KEGGipae:PA5198.
PATRICi19845243. VBIPseAer58763_5448.

Organism-specific databases

PseudoCAPiPA5198.

Phylogenomic databases

eggNOGiENOG4107WMG. Bacteria.
COG1619. LUCA.
HOGENOMiHOG000025480.
InParanoidiQ9HTZ1.
KOiK01297.
OMAiPVIMNHE.
OrthoDBiEOG6JTC7M.
PhylomeDBiQ9HTZ1.

Enzyme and pathway databases

UniPathwayiUPA00544.
BRENDAi3.4.17.13. 5087.

Miscellaneous databases

EvolutionaryTraceiQ9HTZ1.

Family and domain databases

Gene3Di3.40.50.10740. 1 hit.
3.50.30.60. 1 hit.
InterProiIPR027461. Carboxypeptidase_A_C.
IPR029062. Class_I_gatase-like.
IPR027478. LdcA_N_dom.
IPR003507. S66_fam.
[Graphical view]
PfamiPF02016. Peptidase_S66. 1 hit.
[Graphical view]
PIRSFiPIRSF028757. LD-carboxypeptidase. 1 hit.
SUPFAMiSSF141986. SSF141986. 1 hit.
SSF52317. SSF52317. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  2. "Pseudomonas aeruginosa LD-carboxypeptidase, a serine peptidase with a Ser-His-Glu triad and a nucleophilic elbow."
    Korza H.J., Bochtler M.
    J. Biol. Chem. 280:40802-40812(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-115 AND ALA-285, CATALYTIC ACTIVITY, IDENTIFICATION AS A SERINE PEPTIDASE, ACTIVE SITE, SUBUNIT, MUTAGENESIS OF SER-115; GLU-217 AND HIS-285.
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  3. "X-ray crystal structure of hypothetical protein PA5198 at 1.1 A resolution."
    Midwest center for structural genomics (MCSG)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS).

Entry informationi

Entry nameiLDC_PSEAE
AccessioniPrimary (citable) accession number: Q9HTZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: March 1, 2001
Last modified: November 11, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.