PRC_SALTY
ID PRC_SALTY Reviewed; 682 AA.
AC P43669;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 131.
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; OrderedLocusNames=STM1845;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 610-622.
RC STRAIN=ATCC 14028 / Isolate MS4290;
RX PubMed=8168923; DOI=10.1128/iai.62.5.1623-1630.1994;
RA Baumler A.J., Kusters J.G., Stojiljkovic I., Heffron F.;
RT "Salmonella typhimurium loci involved in survival within macrophages.";
RL Infect. Immun. 62:1623-1630(1994).
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 (By similarity). {ECO:0000250}.
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 {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Periplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S41A family. {ECO:0000305}.
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DR EMBL; AE006468; AAL20760.1; -; Genomic_DNA.
DR EMBL; U06136; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_460801.1; NC_003197.2.
DR RefSeq; WP_001091237.1; NC_003197.2.
DR AlphaFoldDB; P43669; -.
DR SMR; P43669; -.
DR STRING; 99287.STM1845; -.
DR MEROPS; S41.001; -.
DR PaxDb; P43669; -.
DR PRIDE; P43669; -.
DR EnsemblBacteria; AAL20760; AAL20760; STM1845.
DR GeneID; 1253364; -.
DR KEGG; stm:STM1845; -.
DR PATRIC; fig|99287.12.peg.1947; -.
DR HOGENOM; CLU_016199_1_0_6; -.
DR OMA; HHYSKPP; -.
DR PhylomeDB; P43669; -.
DR BioCyc; SENT99287:STM1845-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Hydrolase; Membrane; Protease;
KW 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_0000027332"
FT DOMAIN 238..322
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 452
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 463
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 477
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CONFLICT 621..622
FT /note="AL -> SS (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 682 AA; 76779 MW; 052C155E54BB4FD6 CRC64;
MNTFFRLTAL AGLLALAGQS FAVEDITRAD QIPVLKEETQ HATVSERVTS RFTRSHYRQF
DLDEAFSAKI FDRYLNLLDY SHNVLLASDV EQFAKKKTVL GDELRTGKLD VFYDLYNLAQ
KRRFERYQYA LKVLERPMDF TGNDTFNLDR SKAPWPKDEA ELNALWDGKV KFDELSLKLT
GKSDKEIRET LTRRYKFAIR RLAQTNSEDV FSLAMTAFAR EIDPHTNYLS PRNTEQFNTE
MSLSLEGIGA VLQMDDDYTV INSLVAGGPA AKSKSISVGD RIVGVGQAGK PMVDVIGWRL
DDVVALIKGP KGSKVRLEIL PAGKGTKTRI ITLTRERIRL EDRAVKMSVK TVGKEKVGVL
DIPGFYVGLT DDVKVQLQKL EKQNVNSIVI DLRSNGGGAL TEAVSLSGLF IPSGPIVQVR
DNNGKVREDS DTDGVVYYKG PLVVLVDRFS ASASEIFAAA MQDYGRALIV GEPTFGKGTV
QQYRSLNRIY DQMLRPEWPA LGSVQYTIQK FYRVNGGSTQ RKGVTPDIIM PTGNEETETG
EKFEDNALPW DSIDAAKYVK SDDLAPFGPE LLKEHNARIA KDPEFQYIMK DIARFNAMKD
KRNIVSLNYA QREKENNEED ALRLARINDR FKREGKPLLK KLDDLPKDYQ EPDPYLDETV
KIALDLAHLE KEKPAEQAAA NK
