ID   PRC_HAEIN               Reviewed;         695 AA.
AC   P45306;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Tail-specific protease;
DE            EC=3.4.21.102;
DE   AltName: Full=C-terminal-processing peptidase;
DE   AltName: Full=Protease Re;
DE   Flags: Precursor;
GN   Name=prc; OrderedLocusNames=HI_1668;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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; Peripheral membrane protein;
CC       Periplasmic side.
CC   -!- SIMILARITY: Belongs to the peptidase S41A family. {ECO:0000305}.
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DR   EMBL; L42023; AAC23314.1; -; Genomic_DNA.
DR   PIR; F64135; F64135.
DR   RefSeq; NP_439810.1; NC_000907.1.
DR   AlphaFoldDB; P45306; -.
DR   SMR; P45306; -.
DR   STRING; 71421.HI_1668; -.
DR   MEROPS; S41.001; -.
DR   EnsemblBacteria; AAC23314; AAC23314; HI_1668.
DR   KEGG; hin:HI_1668; -.
DR   PATRIC; fig|71421.8.peg.1746; -.
DR   eggNOG; COG0793; Bacteria.
DR   HOGENOM; CLU_016199_1_0_6; -.
DR   OMA; HHYSKPP; -.
DR   PhylomeDB; P45306; -.
DR   BioCyc; HINF71421:G1GJ1-1684-MON; -.
DR   Proteomes; UP000000579; 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..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..695
FT                   /note="Tail-specific protease"
FT                   /id="PRO_0000027333"
FT   DOMAIN          256..316
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   ACT_SITE        459
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        470
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        484
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   695 AA;  78870 MW;  3FB5DECC7E62AC1E CRC64;
     MVMKFKMSKN VICYTWLSVC LSSAIPAFAV QPTLKPSDIS IPAISEESQL ATKRATTRLT
     QSHYRKIKLD DDFSEKIFDR YIKNLDFNHN TFLQSDIDEL RQKYGTKLDE QLNQGDLSAA
     FDIYDVMMKR RYERYTYALS LLDKEPDLNG QDQIEIDREK AAAPQTEADA NKLWDARVKN
     DIINLKLKDK KWSEIKAKLT KRYNLAIRRL TQTKADDIVQ IYLNAFAREI DPHTSYLSPR
     TAKSFNESIN LSLEGIGTTL QSEDDEISIK SLVPGAPAER SKKLHPGDKI IGVGQATGDI
     EDVVGWRLED LVEKIKGKKG TKVRLEIEPA KGGKSRIITL VRDKVRIEDQ AAKLTFEKVS
     GKNIAVIKIP SFYIGLTEDV KKLLVKLENQ KAEALIVDLR ENGGGALTEA VALSGLFITD
     GPVVQVRDAY QRIRVHEDDD ATQQYKGLLF VMINRYSASA SEIFAAAMQD YRRGIIIGQN
     TFGKGTVQQS RSLNFIYDLD QSPLGVLQYT IQKFYRVNGG STQLKGVAAD INFPEIIDAK
     EYGEDKEDNA LAWDKIPSAS YMEVGNINYI DNAVNILNEK HLARIAKDPE FVALNEELKV
     RNERRDRKFL SLNYKMRKAE NDKDDARRLK DLNERFKREG KKALKDIDDL PKDYEAPDFF
     LKEAEKIAAD FVIFNSDQKI NQANGLSEAK TESKK