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 03-AUG-2022, entry version 137.
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.
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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 AlphaFoldDB; P17896; -.
DR SASBDB; P17896; -.
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; BSU_24230.
DR GeneID; 938654; -.
DR KEGG; bsu:BSU24230; -.
DR PATRIC; fig|224308.179.peg.2641; -.
DR eggNOG; COG0750; Bacteria.
DR OMA; TMTFYDP; -.
DR PhylomeDB; P17896; -.
DR BioCyc; BSUB:BSU24230-MON; -.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 1.
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;
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
