CTPA_BACSU
ID CTPA_BACSU Reviewed; 466 AA.
AC O34666; Q45645; Q796B8;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Carboxy-terminal processing protease CtpA;
DE Short=C-terminal processing protease;
DE EC=3.4.21.102;
DE Flags: Precursor;
GN Name=ctpA; Synonyms=orfRM1; OrderedLocusNames=BSU19590;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=168 / PY17;
RX PubMed=8996100; DOI=10.1016/s0378-1119(96)00543-4;
RA Marasco R., Varcamonti M., Ricca E., Sacco M.;
RT "A new Bacillus subtilis gene with homology to Escherichia coli prc.";
RL Gene 183:149-152(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9734814; DOI=10.1093/dnares/5.3.195;
RA Ghim S.-Y., Choi S.-K., Shin B.-S., Jeong Y.-M., Sorokin A., Ehrlich S.D.,
RA Park S.-H.;
RT "Sequence analysis of the Bacillus subtilis 168 chromosome region between
RT the sspC and odhA loci (184 degrees-180 degrees).";
RL DNA Res. 5:195-201(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168 / PY79;
RX PubMed=14526016; DOI=10.1128/jb.185.20.6051-6056.2003;
RA Pan Q., Losick R., Rudner D.Z.;
RT "A second PDZ-containing serine protease contributes to activation of the
RT sporulation transcription factor sigmaK in Bacillus subtilis.";
RL J. Bacteriol. 185:6051-6056(2003).
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 -!- INDUCTION: Is expressed only during vegetative growth.
CC {ECO:0000269|PubMed:8996100}.
CC -!- DISRUPTION PHENOTYPE: Sporulation is not significantly affected.
CC {ECO:0000269|PubMed:14526016}.
CC -!- SIMILARITY: Belongs to the peptidase S41A family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X98341; CAA66987.1; -; Genomic_DNA.
DR EMBL; AF015775; AAB72063.1; -; Genomic_DNA.
DR EMBL; AF006665; AAB81168.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13850.1; -; Genomic_DNA.
DR PIR; B69610; B69610.
DR RefSeq; NP_389840.1; NC_000964.3.
DR RefSeq; WP_003231186.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O34666; -.
DR SMR; O34666; -.
DR STRING; 224308.BSU19590; -.
DR MEROPS; S41.007; -.
DR jPOST; O34666; -.
DR PaxDb; O34666; -.
DR PRIDE; O34666; -.
DR EnsemblBacteria; CAB13850; CAB13850; BSU_19590.
DR GeneID; 940115; -.
DR KEGG; bsu:BSU19590; -.
DR PATRIC; fig|224308.179.peg.2142; -.
DR eggNOG; COG0793; Bacteria.
DR eggNOG; COG3409; Bacteria.
DR InParanoid; O34666; -.
DR OMA; TFNQVDW; -.
DR PhylomeDB; O34666; -.
DR BioCyc; BSUB:BSU19590-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
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; 1.10.101.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR InterPro; IPR005151; Tail-specific_protease.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF47090; SSF47090; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR TIGRFAMs; TIGR00225; prc; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Protease; Reference proteome; Serine protease; Signal.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..466
FT /note="Carboxy-terminal processing protease CtpA"
FT /id="PRO_0000390776"
FT DOMAIN 96..174
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 297
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 308
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 322
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CONFLICT 298..305
FT /note="AAEIMAAA -> RSRNYGRC (in Ref. 1; CAA66987)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 466 AA; 51149 MW; F611AC1121177490 CRC64;
MKRQLKLFFI VLITAVVASA LTLFITGNSS ILGQKSASTG DSKFDKLNKA YEQIKSDYYQ
KTDDDKLVDG AIKGMIQSLD DPYSTYMDQE QAKSFDETIS ASFEGIGAQV EEKDGEILIV
SPIKGSPAEK AGIKPRDQII KVNGKSVKGM NVNEAVALIR GKKGTKVKLE LNRAGVGNID
LSIKRDTIPV ETVYSEMKDN NIGEIQITSF SETTAKELTD AIDSLEKKGA KGYILDLRGN
PGGLMEQAIT MSNLFIDKGK NIMQVEYKNG SKEVMKAEKE RKVTKPTVVL VNDGTASAAE
IMAAALHESS NVPLIGETTF GKGTVQTAKE YDDGSTVKLT VAKWLTADGE WIHKKGIKPQ
VKAELPDYAK LPYLDADKTY KSGDTGTNVK VAQKMLKALG YKVKVNSMYD QDFVSVVKQF
QKKEKLNETG ILTGDTTTKL MIELQKKLSD NDTQMEKAIE TLKKEM
