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Carboxy-terminal processing protease CtpB (C-terminal processing protease) (EC 3.4.21.102)

 CTPB_BACSU              Reviewed;         480 AA.
O35002; Q795D7;
19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 120.
RecName: Full=Carboxy-terminal processing protease CtpB;
Short=C-terminal processing protease;
EC=3.4.21.102 {ECO:0000269|PubMed:24243021};
Flags: Precursor;
Name=ctpB; Synonyms=yvjB; OrderedLocusNames=BSU35240;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9570401; DOI=10.1046/j.1365-2958.1998.00747.x;
Reizer J., Hoischen C., Titgemeyer F., Rivolta C., Rabus R.,
Stuelke J., Karamata D., Saier M.H. Jr., Hillen W.;
"A novel protein kinase that controls carbon catabolite repression in
bacteria.";
Mol. Microbiol. 27:1157-1169(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C.,
Karamata D.;
"Nucleotide sequence of the 300-304 chromosomal segment of Bacillus
subtilis.";
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[4]
FUNCTION IN SIGMA-K ACTIVATION, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
STRAIN=168 / PY79;
PubMed=14526016; DOI=10.1128/JB.185.20.6051-6056.2003;
Pan Q., Losick R., Rudner D.Z.;
"A second PDZ-containing serine protease contributes to activation of
the sporulation transcription factor sigmaK in Bacillus subtilis.";
J. Bacteriol. 185:6051-6056(2003).
[5]
FUNCTION AS A SPOIVFA PROTEASE, AND DISRUPTION PHENOTYPE.
STRAIN=168 / PY79;
PubMed=16818230; DOI=10.1016/j.molcel.2006.05.019;
Campo N., Rudner D.Z.;
"A branched pathway governing the activation of a developmental
transcription factor by regulated intramembrane proteolysis.";
Mol. Cell 23:25-35(2006).
[6]
FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, CLEAVAGE,
CLEAVAGE SITES BY SPOIVB, AND MUTAGENESIS OF 36-ALA--ALA-40.
STRAIN=168 / PY79;
PubMed=17557826; DOI=10.1128/JB.00399-07;
Campo N., Rudner D.Z.;
"SpoIVB and CtpB are both forespore signals in the activation of the
sporulation transcription factor sigmaK in Bacillus subtilis.";
J. Bacteriol. 189:6021-6027(2007).
[7]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 44-480 OF WILD-TYPE AND
MUTANTS TYR-118; ARG-168 AND ALA-309 IN ACTIVE AND RESTING STATES AND
IN COMPLEX WITH PEPTIDE SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY,
ENZYME REGULATION, SUBSTRATE SPECIFICITY, SUBUNIT, DOMAIN, PROTEOLYTIC
AUTO-CLEAVAGE, ACTIVE SITES, SITES, DISRUPTION PHENOTYPE, MUTAGENESIS
OF VAL-118; ARG-168; SER-309 AND GLN-338, AND PDZ DOMAIN DELETION
MUTANT.
PubMed=24243021; DOI=10.1016/j.cell.2013.09.050;
Mastny M., Heuck A., Kurzbauer R., Heiduk A., Boisguerin P.,
Volkmer R., Ehrmann M., Rodrigues C.D., Rudner D.Z., Clausen T.;
"CtpB assembles a gated protease tunnel regulating cell-cell signaling
during spore formation in Bacillus subtilis.";
Cell 155:647-658(2013).
-!- FUNCTION: Involved in the signal transduction pathway leading to
the proteolytic activation of the mother cell transcription factor
pro-sigma-K during sporulation. The signaling serine protease CtpB
triggers pro-sigma-K processing by cleaving the pre-processed
regulatory protein SpoIVFA and is necessary for the proper timing
of sigma-K activation. {ECO:0000269|PubMed:14526016,
ECO:0000269|PubMed:16818230, ECO:0000269|PubMed:17557826,
ECO:0000269|PubMed:24243021}.
-!- 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. {ECO:0000269|PubMed:24243021}.
-!- ENZYME REGULATION: Activated by peptide binding to the PDZ domain.
{ECO:0000269|PubMed:24243021}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24243021}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-5246793, EBI-5246793;
P26936:spoIVFA; NbExp=2; IntAct=EBI-5246793, EBI-5254757;
-!- SUBCELLULAR LOCATION: Forespore intermembrane space
{ECO:0000269|PubMed:17557826}. Note=Is expressed in both the
mother cell and forespore compartments but that synthesis in the
forespore is both necessary and sufficient for the proper timing
of pro-sigma-K processing.
-!- DEVELOPMENTAL STAGE: Is expressed in the forespore under the
control of sigma-G, and in the mother cell under the control of
sigma-E. {ECO:0000269|PubMed:14526016,
ECO:0000269|PubMed:17557826}.
-!- DOMAIN: The PDZ domain functions as a gatekeeper to the protease
tunnel and defines resting and active conformations of the
protease. {ECO:0000269|PubMed:24243021}.
-!- PTM: Is cleaved by SpoIVB in vitro and in vivo but this cleavage
does not appear to be necessary for CtpB activation. CtpB can also
cleave itself in vivo. {ECO:0000269|PubMed:17557826,
ECO:0000269|PubMed:24243021}.
-!- DISRUPTION PHENOTYPE: Pro-sigma-K processing is delayed by
approximately 30 minutes, and sporulation efficiency is reduced
approximately two-fold. {ECO:0000269|PubMed:14526016,
ECO:0000269|PubMed:16818230, ECO:0000269|PubMed:24243021}.
-!- SIMILARITY: Belongs to the peptidase S41A family. {ECO:0000305}.
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EMBL; AF017113; AAC67263.1; -; Genomic_DNA.
EMBL; AL009126; CAB15541.1; -; Genomic_DNA.
PIR; E70042; E70042.
RefSeq; NP_391404.1; NC_000964.3.
RefSeq; WP_003228041.1; NZ_JNCM01000033.1.
PDB; 4C2C; X-ray; 1.90 A; A=44-480.
PDB; 4C2D; X-ray; 2.70 A; A/B/C/D=44-480.
PDB; 4C2E; X-ray; 1.80 A; A/B=44-480.
PDB; 4C2F; X-ray; 2.40 A; A=44-480.
PDB; 4C2G; X-ray; 1.90 A; A=44-480, C=29-40.
PDB; 4C2H; X-ray; 1.95 A; A/B=44-480.
PDBsum; 4C2C; -.
PDBsum; 4C2D; -.
PDBsum; 4C2E; -.
PDBsum; 4C2F; -.
PDBsum; 4C2G; -.
PDBsum; 4C2H; -.
ProteinModelPortal; O35002; -.
SMR; O35002; -.
IntAct; O35002; 3.
STRING; 224308.Bsubs1_010100019066; -.
MEROPS; S41.007; -.
TCDB; 9.B.174.1.1; the two tunnel gated c-terminal processing protease (ctp) family.
PaxDb; O35002; -.
EnsemblBacteria; CAB15541; CAB15541; BSU35240.
GeneID; 936678; -.
KEGG; bsu:BSU35240; -.
PATRIC; fig|224308.179.peg.3814; -.
eggNOG; ENOG4105CN1; Bacteria.
eggNOG; COG0793; LUCA.
HOGENOM; HOG000038765; -.
InParanoid; O35002; -.
OMA; DPHSSYY; -.
PhylomeDB; O35002; -.
BioCyc; BSUB:BSU35240-MONOMER; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
GO; GO:0042277; F:peptide binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
GO; GO:0006518; P:peptide metabolic process; IDA:UniProtKB.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IDA:UniProtKB.
CDD; cd07560; Peptidase_S41_CPP; 1.
Gene3D; 1.10.101.10; -; 1.
InterPro; IPR029045; ClpP/crotonase-like_dom.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
InterPro; IPR004447; Peptidase_S41A.
InterPro; IPR002477; Peptidoglycan-bd-like.
InterPro; IPR036365; PGBD-like_sf.
InterPro; IPR036366; PGBDSf.
InterPro; IPR005151; Tail-specific_protease.
Pfam; PF13180; PDZ_2; 1.
Pfam; PF03572; Peptidase_S41; 1.
Pfam; PF01471; PG_binding_1; 1.
SMART; SM00228; PDZ; 1.
SMART; SM00245; TSPc; 1.
SUPFAM; SSF47090; SSF47090; 1.
SUPFAM; SSF50156; SSF50156; 1.
SUPFAM; SSF52096; SSF52096; 2.
TIGRFAMs; TIGR00225; prc; 1.
PROSITE; PS50106; PDZ; 1.
1: Evidence at protein level;
3D-structure; Autocatalytic cleavage; Complete proteome; Hydrolase;
Protease; Reference proteome; Serine protease; Signal; Sporulation.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 480 Carboxy-terminal processing protease
CtpB.
/FTId=PRO_0000390777.
DOMAIN 92 182 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
REGION 113 116 Peptide binding.
{ECO:0000269|PubMed:24243021}.
ACT_SITE 309 309 Nucleophile.
{ECO:0000269|PubMed:24243021}.
ACT_SITE 334 334 Charge relay system.
{ECO:0000269|PubMed:24243021}.
ACT_SITE 338 338 Charge relay system.
{ECO:0000269|PubMed:24243021}.
SITE 36 37 Cleavage; by SpoIVB, and cleavage; by
autolysis. {ECO:0000269|PubMed:24243021}.
SITE 40 41 Cleavage; by SpoIVB.
SITE 42 43 Cleavage; by autolysis.
{ECO:0000269|PubMed:24243021}.
SITE 168 168 Crucial for substrate binding and
protease activation.
{ECO:0000269|PubMed:24243021}.
MUTAGEN 36 40 AAVPA->RAVPR: No cleavage by SpoIVB. No
effect on pro-sigma-K processing.
{ECO:0000269|PubMed:17557826}.
MUTAGEN 92 182 Missing: Constitutively active protease
with higher activity than wild-type
protease and total loss of substrate
specificity.
{ECO:0000269|PubMed:24243021}.
MUTAGEN 118 118 V->Y: Loss of peptide binding to the PDZ
domain, but still has residual protease
activity. Less than residual protease
activity; when associated with A/F-168.
{ECO:0000269|PubMed:24243021}.
MUTAGEN 168 168 R->A,F: 3- to 5-fold weaker affinity for
PDZ ligands and reduced proteolytic
activity against pre-processed SpoIVFA
substrate. Less than residual protease
activity; when associated with Y-118.
{ECO:0000269|PubMed:24243021}.
MUTAGEN 309 309 S->A: Loss of activity.
{ECO:0000269|PubMed:24243021}.
MUTAGEN 338 338 Q->E: Loss of activity.
{ECO:0000269|PubMed:24243021}.
HELIX 46 65 {ECO:0000244|PDB:4C2E}.
STRAND 66 68 {ECO:0000244|PDB:4C2E}.
HELIX 72 85 {ECO:0000244|PDB:4C2E}.
TURN 86 88 {ECO:0000244|PDB:4C2G}.
STRAND 93 95 {ECO:0000244|PDB:4C2E}.
HELIX 97 108 {ECO:0000244|PDB:4C2E}.
STRAND 109 113 {ECO:0000244|PDB:4C2D}.
STRAND 115 121 {ECO:0000244|PDB:4C2E}.
STRAND 124 130 {ECO:0000244|PDB:4C2E}.
HELIX 135 139 {ECO:0000244|PDB:4C2E}.
STRAND 146 150 {ECO:0000244|PDB:4C2E}.
HELIX 160 167 {ECO:0000244|PDB:4C2E}.
STRAND 174 180 {ECO:0000244|PDB:4C2E}.
STRAND 186 193 {ECO:0000244|PDB:4C2E}.
STRAND 195 198 {ECO:0000244|PDB:4C2C}.
STRAND 202 209 {ECO:0000244|PDB:4C2E}.
STRAND 212 219 {ECO:0000244|PDB:4C2E}.
HELIX 226 239 {ECO:0000244|PDB:4C2E}.
STRAND 245 248 {ECO:0000244|PDB:4C2E}.
HELIX 257 264 {ECO:0000244|PDB:4C2E}.
TURN 265 267 {ECO:0000244|PDB:4C2E}.
STRAND 274 278 {ECO:0000244|PDB:4C2E}.
STRAND 284 287 {ECO:0000244|PDB:4C2E}.
STRAND 299 303 {ECO:0000244|PDB:4C2E}.
HELIX 310 320 {ECO:0000244|PDB:4C2E}.
STRAND 325 329 {ECO:0000244|PDB:4C2E}.
STRAND 336 342 {ECO:0000244|PDB:4C2E}.
STRAND 344 346 {ECO:0000244|PDB:4C2E}.
STRAND 348 357 {ECO:0000244|PDB:4C2E}.
TURN 365 367 {ECO:0000244|PDB:4C2E}.
STRAND 372 374 {ECO:0000244|PDB:4C2E}.
HELIX 379 383 {ECO:0000244|PDB:4C2E}.
HELIX 399 410 {ECO:0000244|PDB:4C2E}.
STRAND 419 421 {ECO:0000244|PDB:4C2E}.
HELIX 424 436 {ECO:0000244|PDB:4C2E}.
STRAND 443 445 {ECO:0000244|PDB:4C2C}.
HELIX 447 462 {ECO:0000244|PDB:4C2E}.
HELIX 464 466 {ECO:0000244|PDB:4C2E}.
HELIX 468 476 {ECO:0000244|PDB:4C2E}.
SEQUENCE 480 AA; 52798 MW; 902B082C85B5CEC4 CRC64;
MNQKIMAVIA AGSMLFGGAG VYAGINLLEM DKPQTAAVPA TAQADSERDK AMDKIEKAYE
LISNEYVEKV DREKLLEGAI QGMLSTLNDP YSVYMDKQTA KQFSDSLDSS FEGIGAEVGM
EDGKIIIVSP FKKSPAEKAG LKPNDEIISI NGESMAGKDL NHAVLKIRGK KGSSVSMKIQ
RPGTKKQLSF RIKRAEIPLE TVFASEKKVQ GHSVGYIAIS TFSEHTAEDF AKALRELEKK
EIEGLVIDVR GNPGGYLQSV EEILKHFVTK DQPYIQIAER NGDKKRYFST LTHKKAYPVN
VITDKGSASA SEILAGALKE AGHYDVVGDT SFGKGTVQQA VPMGDGSNIK LTLYKWLTPN
GNWIHKKGIE PTIAIKQPDY FSAGPLQLKE PLKVDMNNED VKHAQVLLKG LSFDPGREDG
YFSKDMKKAV MAFQDQNKLN KTGVIDTRTA ETLNQQIEKK KSDEKNDLQL QTALKSLFVN


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