Tail-specific protease precursor - Escherichia coli (strain K12)

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P23865 (PRC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 122. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Tail-specific protease
EC=3.4.21.102

Alternative name(s):
C-terminal-processing peptidase
PRC protein
Protease Re

Gene names

Name:	prc
Synonyms:	tsp
Ordered Locus Names:	b1830, JW1819

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	682 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). May be involved in protection of the bacterium from thermal and osmotic stresses.
Catalytic activity	The enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-\|-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala.
Subcellular location	Cell inner membrane; Peripheral membrane protein; Periplasmic side.
Sequence similarities	Belongs to the peptidase S41A family. Contains 1 PDZ (DHR) domain.
Sequence caution	The sequence BAA00578.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein catabolic process Inferred from direct assay PubMed 8520476. Source: EcoliWiki proteolysis Inferred from direct assay PubMed 8520476. Source: EcoliWiki response to drug Inferred from experiment Ref.6. Source: EcoCyc
Cellular_component	outer membrane-bounded periplasmic space Inferred from direct assay Ref.1. Source: EcoCyc plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	endopeptidase activity Inferred from direct assay PubMed 8520476. Source: EcoliWiki serine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

Potential

Chain

23 – 682

660

Tail-specific protease

PRO_0000027331

Regions

Domain

238 – 322

PDZ

Sites

Active site

452

Charge relay system Ref.8

Active site

463

Charge relay system Probable

Active site

477

Charge relay system Ref.8

Experimental info

Mutagenesis

397

G → A: Loss of activity. Perturbs protein structure. Ref.8

Mutagenesis

398

G → A: Loss of activity. Perturbs protein structure. Ref.8

Mutagenesis

452

S → A: Loss of activity. Ref.8

Mutagenesis

452

S → C: Reduces activity by over 90%. Ref.8

Mutagenesis

455

E → A: Loss of activity. Perturbs protein structure. Ref.8

Mutagenesis

463

D → A: Loss of activity. Ref.8

Mutagenesis

463

D → N: Reduces activity by 90%. Ref.8

Mutagenesis

474

T → A: Loss of activity. Perturbs protein structure. Ref.8

Mutagenesis

477

K → A or H: Loss of activity. No apparent effect on protein structure. Ref.8

Mutagenesis

477

K → R: Loss of activity. Perturbs protein structure. Ref.8

Sequence conflict

317

L → Q in BAA00577. Ref.1

Sequence conflict

317

L → Q in BAA00578. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P23865 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 49D1DE9574CCD4BB
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FASTA

682

76,663

        10         20         30         40         50         60 
MNMFFRLTAL AGLLAIAGQT FAVEDITRAD QIPVLKEETQ HATVSERVTS RFTRSHYRQF 

        70         80         90        100        110        120 
DLDQAFSAKI FDRYLNLLDY SHNVLLASDV EQFAKKKTEL GDELRSGKLD VFYDLYNLAQ 

       130        140        150        160        170        180 
KRRFERYQYA LSVLEKPMDF TGNDTYNLDR SKAPWPKNEA ELNALWDSKV KFDELSLKLT 

       190        200        210        220        230        240 
GKTDKEIRET LTRRYKFAIR RLAQTNSEDV FSLAMTAFAR EIDPHTNYLS PRNTEQFNTE 

       250        260        270        280        290        300 
MSLSLEGIGA VLQMDDDYTV INSMVAGGPA AKSKAISVGD KIVGVGQTGK PMVDVIGWRL 

       310        320        330        340        350        360 
DDVVALIKGP KGSKVRLEIL PAGKGTKTRT VTLTRERIRL EDRAVKMSVK TVGKEKVGVL 

       370        380        390        400        410        420 
DIPGFYVGLT DDVKVQLQKL EKQNVSSVII DLRSNGGGAL TEAVSLSGLF IPAGPIVQVR 

       430        440        450        460        470        480 
DNNGKVREDS DTDGQVFYKG PLVVLVDRFS ASASEIFAAA MQDYGRALVV GEPTFGKGTV 

       490        500        510        520        530        540 
QQYRSLNRIY DQMLRPEWPA LGSVQYTIQK FYRVNGGSTQ RKGVTPDIIM PTGNEETETG 

       550        560        570        580        590        600 
EKFEDNALPW DSIDAATYVK SGDLTAFEPE LLKEHNARIA KDPEFQNIMK DIARFNAMKD 

       610        620        630        640        650        660 
KRNIVSLNYA VREKENNEDD ATRLARLNER FKREGKPELK KLDDLPKDYQ EPDPYLDETV 

       670        680 
NIALDLAKLE KARPAEQPAP VK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, mapping, and characterization of the Escherichia coli prc gene, which is involved in C-terminal processing of penicillin-binding protein 3." Hara H., Yamamoto Y., Higashitani A., Suzuki H., Nishimura Y. J. Bacteriol. 173:4799-4813(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"Tsp: a tail-specific protease that selectively degrades proteins with nonpolar C termini." Silber K.R., Keiler K.C., Sauer R.T. Proc. Natl. Acad. Sci. U.S.A. 89:295-299(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. Horiuchi T. DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Multiple antibiotic susceptibility associated with inactivation of the prc gene." Seoane A., Sabbaj A., McMurry L.M., Levy S.B. J. Bacteriol. 174:7844-7847(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 330-403.
[7]	"Protein ProQ influences osmotic activation of compatible solute transporter ProP in Escherichia coli K-12." Kunte H.J., Crane R.A., Culham D.E., Richmond D., Wood J.M. J. Bacteriol. 181:1537-1543(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33. Strain: K12.
[8]	"Identification of active site residues of the Tsp protease." Keiler K.C., Sauer R.T. J. Biol. Chem. 270:28864-28868(1995) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF GLY-397; GLY-398; SER-452; GLU-455; ASP-463; THR-474 AND LYS-477, IDENTIFICATION OF ACTIVE SITE RESIDUES.
[9]	"Sequence determinants of C-terminal substrate recognition by the Tsp protease." Keiler K.C., Sauer R.T. J. Biol. Chem. 271:2589-2593(1996) [PubMed] [Europe PMC] [Abstract] Cited for: SUBSTRATE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D00674 Genomic DNA. Translation: BAA00577.1. D00674 Genomic DNA. Translation: BAA00578.1. Different initiation. M75634 Genomic DNA. Translation: AAA24699.1. U00096 Genomic DNA. Translation: AAC74900.1. AP009048 Genomic DNA. Translation: BAA15638.1. S49803 Genomic DNA. Translation: AAB24313.1. L48409 Genomic DNA. Translation: AAD41528.1.
PIR	A41798.
RefSeq	NP_416344.1. NC_000913.2. YP_490092.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P23865.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-10557N.
IntAct	P23865. 3 interactions.
MINT	MINT-1283244.
STRING	511145.b1830.
Protein family/group databases
MEROPS	S41.001.
Proteomic databases
PaxDb	P23865.
PRIDE	P23865.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC74900; AAC74900; b1830. BAA15638; BAA15638; BAA15638.
GeneID	12934469. 946096.
KEGG	ecj:Y75_p1806. eco:b1830.
PATRIC	32118981. VBIEscCol129921_1908.
Organism-specific databases
EchoBASE	EB0753.
EcoGene	EG10760. prc.
Phylogenomic databases
eggNOG	COG0793.
HOGENOM	HOG000277886.
KO	K03797.
OMA	GHVQYTI.
ProtClustDB	PRK11186.
Enzyme and pathway databases
BioCyc	EcoCyc:EG10760-MONOMER. ECOL316407:JW1819-MONOMER. MetaCyc:EG10760-MONOMER.
Gene expression databases
Genevestigator	P23865.
Family and domain databases
InterPro	IPR005151. Interphotoreceptor_retinol-bd. IPR001478. PDZ. IPR004447. Peptidase_S41A. IPR020992. Tail_Prtase_C. [Graphical view]
Pfam	PF11818. DUF3340. 1 hit. PF00595. PDZ. 1 hit. PF03572. Peptidase_S41. 1 hit. [Graphical view]
SMART	SM00228. PDZ. 1 hit. SM00245. TSPc. 1 hit. [Graphical view]
SUPFAM	SSF50156. PDZ. 1 hit.
TIGRFAMs	TIGR00225. prc. 1 hit.
PROSITE	PS50106. PDZ. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PRC_ECOLI

Accession

Primary (citable) accession number: P23865

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents