(data stored in SCRATCH zone)

SWISSPROT: SP4B_BACSU

ID   SP4B_BACSU              Reviewed;         426 AA.
AC   P17896;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   11-DEC-2019, entry version 128.
DE   RecName: Full=SpoIVB peptidase;
DE            EC=3.4.21.116;
DE   AltName: Full=Sporulation factor IV B protease;
DE   AltName: Full=Stage IV sporulation protein B;
DE   Contains:
DE     RecName: Full=SpoIVB peptidase 45 kDa isoform;
DE   Contains:
DE     RecName: Full=SpoIVB peptidase 43 kDa isoform;
DE   Contains:
DE     RecName: Full=SpoIVB peptidase 42 kDa isoform;
DE   Flags: Precursor;
GN   Name=spoIVB; OrderedLocusNames=BSU24230;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / PY79;
RX   PubMed=2106508; DOI=10.1128/jb.172.3.1306-1311.1990;
RA   van Hoy B.E., Hoch J.A.;
RT   "Characterization of the spoIVB and recN loci of Bacillus subtilis.";
RL   J. Bacteriol. 172:1306-1311(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
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   SEQUENCE REVISION TO 125.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
RP   CHARACTERIZATION, PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, AND MUTAGENESIS
RP   OF CYS-23 AND SER-378.
RC   STRAIN=168 / PY79;
RX   PubMed=10931284; DOI=10.1046/j.1365-2958.2000.01946.x;
RA   Wakeley P.R., Dorazi R., Hoa N.T., Bowyer J.R., Cutting S.M.;
RT   "Proteolysis of SpolVB is a critical determinant in signalling of Pro-
RT   sigmaK processing in Bacillus subtilis.";
RL   Mol. Microbiol. 36:1336-1348(2000).
RN   [6]
RP   CHARACTERIZATION, FUNCTION, AND MUTAGENESIS OF ASP-213; HIS-236; ASP-240;
RP   ASP-242; ASN-290; LYS-321; ASP-363; SER-378; LYS-387 AND HIS-394.
RC   STRAIN=168 / PY79;
RX   PubMed=11741860; DOI=10.1128/jb.184.1.191-199.2002;
RA   Hoa N.T., Brannigan J.A., Cutting S.M.;
RT   "The Bacillus subtilis signaling protein SpoIVB defines a new family of
RT   serine peptidases.";
RL   J. Bacteriol. 184:191-199(2002).
RN   [7]
RP   CHARACTERIZATION.
RC   STRAIN=168 / PY79;
RX   PubMed=12940997; DOI=10.1046/j.1365-2958.2003.03651.x;
RA   Dong T.C., Cutting S.M.;
RT   "SpoIVB-mediated cleavage of SpoIVFA could provide the intercellular signal
RT   to activate processing of Pro-sigmaK in Bacillus subtilis.";
RL   Mol. Microbiol. 49:1425-1434(2003).
RN   [8]
RP   CHARACTERIZATION, AND MUTAGENESIS OF THR-393 AND VAL-395.
RC   STRAIN=168 / PY79;
RX   PubMed=15292188; DOI=10.1074/jbc.m407048200;
RA   Dong T.C., Cutting S.M.;
RT   "The PDZ domain of the SpoIVB transmembrane signaling protein enables cis-
RT   trans interactions involving multiple partners leading to the activation of
RT   the pro-sigmaK processing complex in Bacillus subtilis.";
RL   J. Biol. Chem. 279:43468-43478(2004).
CC   -!- FUNCTION: Plays a central role in the sigma-K checkpoint which
CC       coordinates gene expression during the later stages of spore formation.
CC       The protease is activated by trans cleavage of the zymogen precursor
CC       producing SpoIVB-45 kDa. This undergoes further trimming by cis
CC       cleavage to form SpoIVB-43 kDa and SpoIVB-42 kDa. The protease then
CC       cleaves the C-terminus of the SpoIVFA metalloprotease activating the
CC       latter. {ECO:0000269|PubMed:10931284, ECO:0000269|PubMed:11741860}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Self-cleaves 52-Val-|-Asn-53, 62-Ala-|-Phe-63 and 74-Val-|-
CC         Thr-75 at the N-terminus of SpoIVB.; EC=3.4.21.116;
CC   -!- ACTIVITY REGULATION: The zymogen is inhibited from undergoing
CC       autoactivation by BofC. The protease is inactivated by proteolytic
CC       cleavage.
CC   -!- SUBUNIT: The PDZ domain mediates interaction with another SpoIVB
CC       protein during transactivation. Also mediates interaction with BofA
CC       during cleavage of SpoIVFA.
CC   -!- SUBCELLULAR LOCATION: Forespore intermembrane space.
CC   -!- DEVELOPMENTAL STAGE: Transcribed in low amounts by sigma-F. Transcribed
CC       during stage III of sporogenesis by sigma-G.
DR   EMBL; M30297; AAA22692.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12580.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14354.2; -; Genomic_DNA.
DR   PIR; C35128; C35128.
DR   RefSeq; NP_390303.2; NC_000964.3.
DR   RefSeq; WP_004398697.1; NZ_JNCM01000036.1.
DR   RefSeq; WP_009967699.1; NZ_CM000487.1.
DR   SMR; P17896; -.
DR   IntAct; P17896; 1.
DR   STRING; 224308.BSU24230; -.
DR   MEROPS; S55.001; -.
DR   PaxDb; P17896; -.
DR   PRIDE; P17896; -.
DR   EnsemblBacteria; CAB14354; CAB14354; BSU24230.
DR   GeneID; 938654; -.
DR   KEGG; bsu:BSU24230; -.
DR   PATRIC; fig|224308.179.peg.2641; -.
DR   eggNOG; ENOG4105S1Z; Bacteria.
DR   eggNOG; COG0750; LUCA.
DR   HOGENOM; HOG000057628; -.
DR   KO; K06399; -.
DR   OMA; TMTFYDP; -.
DR   PhylomeDB; P17896; -.
DR   BioCyc; BSUB:BSU24230-MONOMER; -.
DR   BRENDA; 3.4.21.116; 658.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR014219; Pept_S55_SpoIVB.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR008763; Peptidase_S55.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF05580; Peptidase_S55; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   TIGRFAMs; TIGR02860; spore_IV_B; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS51494; SPOIVB; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P17896.
DR   SWISS-2DPAGE; P17896.
KW   Direct protein sequencing; Hydrolase; Protease; Reference proteome;
KW   Serine protease; Signal; Sporulation; Zymogen.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   PROPEP          29..52
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:10931284"
FT                   /id="PRO_0000045844"
FT   CHAIN           53..426
FT                   /note="SpoIVB peptidase 45 kDa isoform"
FT                   /id="PRO_0000045845"
FT   CHAIN           63..426
FT                   /note="SpoIVB peptidase 43 kDa isoform"
FT                   /id="PRO_0000045846"
FT   CHAIN           75..426
FT                   /note="SpoIVB peptidase 42 kDa isoform"
FT                   /id="PRO_0000045847"
FT   DOMAIN          101..187
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          188..426
FT                   /note="Peptidase S55"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00827"
FT   REGION          393..395
FT                   /note="PDZ binding"
FT   ACT_SITE        236
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        363
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        378
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         23
FT                   /note="C->S: No effect."
FT                   /evidence="ECO:0000269|PubMed:10931284"
FT   MUTAGEN         213
FT                   /note="D->L: No effect."
FT                   /evidence="ECO:0000269|PubMed:11741860"
FT   MUTAGEN         236
FT                   /note="H->F,N: Inhibits spore formation."
FT                   /evidence="ECO:0000269|PubMed:11741860"
FT   MUTAGEN         240
FT                   /note="D->L: No effect."
FT                   /evidence="ECO:0000269|PubMed:11741860"
FT   MUTAGEN         242
FT                   /note="D->L: Inhibits spore formation."
FT                   /evidence="ECO:0000269|PubMed:11741860"
FT   MUTAGEN         242
FT                   /note="D->N: No effect."
FT                   /evidence="ECO:0000269|PubMed:11741860"
FT   MUTAGEN         290
FT                   /note="N->I: Sporulation deficient spores."
FT                   /evidence="ECO:0000269|PubMed:11741860"
FT   MUTAGEN         321
FT                   /note="K->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:11741860"
FT   MUTAGEN         363
FT                   /note="D->L: Inhibits spore formation."
FT                   /evidence="ECO:0000269|PubMed:11741860"
FT   MUTAGEN         363
FT                   /note="D->N: No effect."
FT                   /evidence="ECO:0000269|PubMed:11741860"
FT   MUTAGEN         378
FT                   /note="S->A,K: Inhibits autoproteolysis of protein and
FT                   spore formation."
FT                   /evidence="ECO:0000269|PubMed:10931284,
FT                   ECO:0000269|PubMed:11741860"
FT   MUTAGEN         387
FT                   /note="K->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:11741860"
FT   MUTAGEN         393
FT                   /note="T->I,N: Reduced binding to PDZ domain and
FT                   sporulation deficient spores."
FT                   /evidence="ECO:0000269|PubMed:15292188"
FT   MUTAGEN         394
FT                   /note="H->D: Sporulation deficient spores."
FT                   /evidence="ECO:0000269|PubMed:11741860"
FT   MUTAGEN         395
FT                   /note="V->E: Reduced binding to PDZ domain and sporulation
FT                   deficient spores."
FT                   /evidence="ECO:0000269|PubMed:15292188"
FT   CONFLICT        125
FT                   /note="Missing (in Ref. 1; AAA22692 and 2; BAA12580)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   426 AA;  46075 MW;  8BA00732B9D12271 CRC64;
     MPDNIRKAVG LILLVSLLSV GLCKPLKEYL LIPTQMRVFE TQTQAIETSL SVNAQTSESS
     EAFTVKKDPH EIKVTGKKSG ESELVYDLAG FPIKKTKVHV LPDLKVIPGG QSIGVKLHSV
     GVLVVGFHQI NTSEGKKSPG ETAGIEAGDI IIEMNGQKIE KMNDVAPFIQ KAGKTGESLD
     LLIKRDKQKI KTKLIPEKDE GEGKYRIGLY IRDSAAGIGT MTFYEPKTKK YGALGHVISD
     MDTKKPIVVE NGEIVKSTVT SIEKGTGGNP GEKLARFSSE RKTIGDINRN SPFGIFGTLH
     QPIQNNISDQ ALPVAFSTEV KKGPAEILTV IDDDKVEKFD IEIVSTTPQK FPATKGMVLK
     ITDPRLLKET GGIVQGMSGS PIIQNGKVIG AVTHVFVNDP TSGYGVHIEW MLSEAGIDIY
     GKEKAS
//

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