PRC_ECOLI
ID PRC_ECOLI Reviewed; 682 AA.
AC P23865;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Tail-specific protease;
DE EC=3.4.21.102;
DE AltName: Full=C-terminal-processing peptidase;
DE AltName: Full=PRC protein;
DE AltName: Full=Protease Re;
DE Flags: Precursor;
GN Name=prc; Synonyms=tsp; OrderedLocusNames=b1830, JW1819;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=1856173; DOI=10.1128/jb.173.15.4799-4813.1991;
RA Hara H., Yamamoto Y., Higashitani A., Suzuki H., Nishimura Y.;
RT "Cloning, mapping, and characterization of the Escherichia coli prc gene,
RT which is involved in C-terminal processing of penicillin-binding protein
RT 3.";
RL J. Bacteriol. 173:4799-4813(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1729701; DOI=10.1073/pnas.89.1.295;
RA Silber K.R., Keiler K.C., Sauer R.T.;
RT "Tsp: a tail-specific protease that selectively degrades proteins with
RT nonpolar C termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:295-299(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 330-403.
RX PubMed=1447154; DOI=10.1128/jb.174.23.7844-7847.1992;
RA Seoane A., Sabbaj A., McMurry L.M., Levy S.B.;
RT "Multiple antibiotic susceptibility associated with inactivation of the prc
RT gene.";
RL J. Bacteriol. 174:7844-7847(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
RC STRAIN=K12;
RX PubMed=10049386; DOI=10.1128/jb.181.5.1537-1543.1999;
RA Kunte H.J., Crane R.A., Culham D.E., Richmond D., Wood J.M.;
RT "Protein ProQ influences osmotic activation of compatible solute
RT transporter ProP in Escherichia coli K-12.";
RL J. Bacteriol. 181:1537-1543(1999).
RN [8]
RP MUTAGENESIS OF GLY-397; GLY-398; SER-452; GLU-455; ASP-463; THR-474 AND
RP LYS-477, AND IDENTIFICATION OF ACTIVE SITE RESIDUES.
RX PubMed=7499412; DOI=10.1074/jbc.270.48.28864;
RA Keiler K.C., Sauer R.T.;
RT "Identification of active site residues of the Tsp protease.";
RL J. Biol. Chem. 270:28864-28868(1995).
RN [9]
RP SUBSTRATE SPECIFICITY.
RX PubMed=8576225; DOI=10.1074/jbc.271.5.2589;
RA Keiler K.C., Sauer R.T.;
RT "Sequence determinants of C-terminal substrate recognition by the Tsp
RT protease.";
RL J. Biol. Chem. 271:2589-2593(1996).
CC -!- FUNCTION: Involved in the cleavage of a C-terminal peptide of 11
CC residues from the precursor form of penicillin-binding protein 3
CC (PBP3). May be involved in protection of the bacterium from thermal and
CC osmotic stresses.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=The enzyme shows specific recognition of a C-terminal
CC tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa
CC is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves
CC at a variable distance from the C-terminus. A typical cleavage is
CC -Ala-Ala-|-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala.;
CC EC=3.4.21.102;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein;
CC Periplasmic side.
CC -!- SIMILARITY: Belongs to the peptidase S41A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA00578.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D00674; BAA00577.1; -; Genomic_DNA.
DR EMBL; D00674; BAA00578.1; ALT_INIT; Genomic_DNA.
DR EMBL; M75634; AAA24699.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74900.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15638.1; -; Genomic_DNA.
DR EMBL; S49803; AAB24313.1; -; Genomic_DNA.
DR EMBL; L48409; AAD41528.1; -; Genomic_DNA.
DR PIR; A41798; A41798.
DR RefSeq; NP_416344.1; NC_000913.3.
DR RefSeq; WP_001055791.1; NZ_SSZK01000001.1.
DR PDB; 5WQL; X-ray; 2.30 A; C/D=1-682.
DR PDB; 6IQQ; X-ray; 2.80 A; C/D=1-682.
DR PDB; 6IQR; X-ray; 3.42 A; A/B=1-682.
DR PDB; 6IQS; X-ray; 2.69 A; C/D=1-682.
DR PDB; 6IQU; X-ray; 2.90 A; B=1-246, B=340-682.
DR PDBsum; 5WQL; -.
DR PDBsum; 6IQQ; -.
DR PDBsum; 6IQR; -.
DR PDBsum; 6IQS; -.
DR PDBsum; 6IQU; -.
DR AlphaFoldDB; P23865; -.
DR SMR; P23865; -.
DR BioGRID; 4263463; 512.
DR DIP; DIP-10557N; -.
DR IntAct; P23865; 3.
DR STRING; 511145.b1830; -.
DR MEROPS; S41.001; -.
DR TCDB; 9.B.174.1.2; the two tunnel gated c-terminal processing protease (ctp) family.
DR jPOST; P23865; -.
DR PaxDb; P23865; -.
DR PRIDE; P23865; -.
DR EnsemblBacteria; AAC74900; AAC74900; b1830.
DR EnsemblBacteria; BAA15638; BAA15638; BAA15638.
DR GeneID; 58462260; -.
DR GeneID; 946096; -.
DR KEGG; ecj:JW1819; -.
DR KEGG; eco:b1830; -.
DR PATRIC; fig|511145.12.peg.1908; -.
DR EchoBASE; EB0753; -.
DR eggNOG; COG0793; Bacteria.
DR HOGENOM; CLU_016199_1_0_6; -.
DR InParanoid; P23865; -.
DR OMA; HHYSKPP; -.
DR PhylomeDB; P23865; -.
DR BioCyc; EcoCyc:EG10760-MON; -.
DR BioCyc; MetaCyc:EG10760-MON; -.
DR BRENDA; 3.4.21.102; 2026.
DR PRO; PR:P23865; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004175; F:endopeptidase activity; IDA:EcoliWiki.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030163; P:protein catabolic process; IDA:EcoliWiki.
DR GO; GO:0006508; P:proteolysis; IDA:EcoliWiki.
DR GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd07560; Peptidase_S41_CPP; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR005151; Tail-specific_protease.
DR InterPro; IPR020992; Tail_Prtase_C.
DR InterPro; IPR040573; TSP_N.
DR Pfam; PF11818; DUF3340; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR Pfam; PF17804; TSP_NTD; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR TIGRFAMs; TIGR00225; prc; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Protease; Reference proteome; Serine protease; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..682
FT /note="Tail-specific protease"
FT /id="PRO_0000027331"
FT DOMAIN 238..322
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 635..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 452
FT /note="Charge relay system"
FT ACT_SITE 463
FT /note="Charge relay system"
FT /evidence="ECO:0000305"
FT ACT_SITE 477
FT /note="Charge relay system"
FT MUTAGEN 397
FT /note="G->A: Loss of activity. Perturbs protein structure."
FT /evidence="ECO:0000269|PubMed:7499412"
FT MUTAGEN 398
FT /note="G->A: Loss of activity. Perturbs protein structure."
FT /evidence="ECO:0000269|PubMed:7499412"
FT MUTAGEN 452
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7499412"
FT MUTAGEN 452
FT /note="S->C: Reduces activity by over 90%."
FT /evidence="ECO:0000269|PubMed:7499412"
FT MUTAGEN 455
FT /note="E->A: Loss of activity. Perturbs protein structure."
FT /evidence="ECO:0000269|PubMed:7499412"
FT MUTAGEN 463
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7499412"
FT MUTAGEN 463
FT /note="D->N: Reduces activity by 90%."
FT /evidence="ECO:0000269|PubMed:7499412"
FT MUTAGEN 474
FT /note="T->A: Loss of activity. Perturbs protein structure."
FT /evidence="ECO:0000269|PubMed:7499412"
FT MUTAGEN 477
FT /note="K->A,H: Loss of activity. No apparent effect on
FT protein structure."
FT /evidence="ECO:0000269|PubMed:7499412"
FT MUTAGEN 477
FT /note="K->R: Loss of activity. Perturbs protein structure."
FT /evidence="ECO:0000269|PubMed:7499412"
FT CONFLICT 317
FT /note="L -> Q (in Ref. 1; BAA00577/BAA00578)"
FT /evidence="ECO:0000305"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:5WQL"
FT HELIX 41..54
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:6IQU"
FT HELIX 64..78
FT /evidence="ECO:0007829|PDB:5WQL"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:6IQR"
FT HELIX 87..94
FT /evidence="ECO:0007829|PDB:5WQL"
FT HELIX 95..99
FT /evidence="ECO:0007829|PDB:5WQL"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:5WQL"
FT HELIX 110..134
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:5WQL"
FT HELIX 159..178
FT /evidence="ECO:0007829|PDB:5WQL"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:5WQL"
FT HELIX 184..203
FT /evidence="ECO:0007829|PDB:5WQL"
FT HELIX 207..222
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:5WQL"
FT HELIX 231..242
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 249..257
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:5WQL"
FT TURN 269..272
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 281..290
FT /evidence="ECO:0007829|PDB:5WQL"
FT HELIX 300..307
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 314..320
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:5WQL"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 346..352
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 355..361
FT /evidence="ECO:0007829|PDB:5WQL"
FT HELIX 369..382
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 386..391
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:5WQL"
FT HELIX 400..408
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 413..420
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 442..446
FT /evidence="ECO:0007829|PDB:5WQL"
FT HELIX 453..463
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 467..472
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 479..485
FT /evidence="ECO:0007829|PDB:5WQL"
FT HELIX 491..494
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 503..512
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:6IQS"
FT TURN 520..522
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 527..529
FT /evidence="ECO:0007829|PDB:5WQL"
FT HELIX 531..534
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:6IQQ"
FT HELIX 541..543
FT /evidence="ECO:0007829|PDB:5WQL"
FT HELIX 565..567
FT /evidence="ECO:0007829|PDB:5WQL"
FT HELIX 568..580
FT /evidence="ECO:0007829|PDB:5WQL"
FT HELIX 583..598
FT /evidence="ECO:0007829|PDB:5WQL"
FT HELIX 599..601
FT /evidence="ECO:0007829|PDB:5WQL"
FT STRAND 604..606
FT /evidence="ECO:0007829|PDB:5WQL"
FT HELIX 609..633
FT /evidence="ECO:0007829|PDB:5WQL"
FT HELIX 642..644
FT /evidence="ECO:0007829|PDB:5WQL"
FT HELIX 654..670
FT /evidence="ECO:0007829|PDB:5WQL"
SQ SEQUENCE 682 AA; 76663 MW; 49D1DE9574CCD4BB CRC64;
MNMFFRLTAL AGLLAIAGQT FAVEDITRAD QIPVLKEETQ HATVSERVTS RFTRSHYRQF
DLDQAFSAKI FDRYLNLLDY SHNVLLASDV EQFAKKKTEL GDELRSGKLD VFYDLYNLAQ
KRRFERYQYA LSVLEKPMDF TGNDTYNLDR SKAPWPKNEA ELNALWDSKV KFDELSLKLT
GKTDKEIRET LTRRYKFAIR RLAQTNSEDV FSLAMTAFAR EIDPHTNYLS PRNTEQFNTE
MSLSLEGIGA VLQMDDDYTV INSMVAGGPA AKSKAISVGD KIVGVGQTGK PMVDVIGWRL
DDVVALIKGP KGSKVRLEIL PAGKGTKTRT VTLTRERIRL EDRAVKMSVK TVGKEKVGVL
DIPGFYVGLT DDVKVQLQKL EKQNVSSVII DLRSNGGGAL TEAVSLSGLF IPAGPIVQVR
DNNGKVREDS DTDGQVFYKG PLVVLVDRFS ASASEIFAAA MQDYGRALVV GEPTFGKGTV
QQYRSLNRIY DQMLRPEWPA LGSVQYTIQK FYRVNGGSTQ RKGVTPDIIM PTGNEETETG
EKFEDNALPW DSIDAATYVK SGDLTAFEPE LLKEHNARIA KDPEFQNIMK DIARFNAMKD
KRNIVSLNYA VREKENNEDD ATRLARLNER FKREGKPELK KLDDLPKDYQ EPDPYLDETV
NIALDLAKLE KARPAEQPAP VK
