HTRB_BACSU
ID HTRB_BACSU Reviewed; 458 AA.
AC Q9R9I1; O35021; O35039;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Serine protease Do-like HtrB;
DE EC=3.4.21.107;
DE AltName: Full=HtrA-like serine protease;
GN Name=htrB; Synonyms=yvtA; OrderedLocusNames=BSU33000;
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;
RX PubMed=10692364; DOI=10.1128/jb.182.6.1592-1599.2000;
RA Noone D., Howell A., Devine K.M.;
RT "Expression of ykdA, encoding a Bacillus subtilis homologue of HtrA, is
RT heat shock inducible and negatively autoregulated.";
RL J. Bacteriol. 182:1592-1599(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9353931; DOI=10.1099/00221287-143-10-3305;
RA Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J.;
RT "Sequencing of regions downstream of addA (98 degrees) and citG (289
RT degrees) in Bacillus subtilis.";
RL Microbiology 143:3305-3308(1997).
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.
RX PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA Medigue C., Rose M., Viari A., Danchin A.;
RT "Detecting and analyzing DNA sequencing errors: toward a higher quality of
RT the Bacillus subtilis genome sequence.";
RL Genome Res. 9:1116-1127(1999).
RN [5]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=11133960; DOI=10.1128/jb.183.2.654-663.2001;
RA Noone D., Howell A., Collery R., Devine K.M.;
RT "YkdA and YvtA, HtrA-like serine proteases in Bacillus subtilis, engage in
RT negative autoregulation and reciprocal cross-regulation of ykdA and yvtA
RT gene expression.";
RL J. Bacteriol. 183:654-663(2001).
CC -!- FUNCTION: Degrades abnormal exported proteins and responsible for the
CC propeptide processing of a natural pro-protein and for the maturation
CC of a native protein. It also plays a prominent role in stress (heat
CC shock, ethanol, puromycin and NaCl) resistance during active
CC exponential growth (Probable). {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Acts on substrates that are at least partially unfolded. The
CC cleavage site P1 residue is normally between a pair of hydrophobic
CC residues, such as Val-|-Val.; EC=3.4.21.107;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Induced by heat shock during exponential growth and by
CC heterologous amylases at the transition phase of the growth cycle.
CC Negatively regulates its own expression. {ECO:0000269|PubMed:11133960}.
CC -!- DISRUPTION PHENOTYPE: In contrast to other bacteria, in which
CC inactivation of serine protease leads to thermosensitivity,
CC inactivation of HtrB leads to an increased thermotolerance and an
CC increased tolerance to hydrogen peroxide. Inactivation of both HtrA and
CC HtrB leads to growth defects and to thermosensitivity.
CC {ECO:0000269|PubMed:11133960}.
CC -!- MISCELLANEOUS: Inactivation results in compensating overexpression of
CC YkdA, especially during stress conditions.
CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB07968.1; Type=Frameshift; Note=Produces two separate ORFs.; Evidence={ECO:0000305};
CC Sequence=CAB07969.1; Type=Frameshift; Note=Produces two separate ORFs.; Evidence={ECO:0000305};
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DR EMBL; AF188296; AAF03153.1; -; Genomic_DNA.
DR EMBL; Z93941; CAB07968.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z93941; CAB07969.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAB15290.2; -; Genomic_DNA.
DR PIR; E70048; E70048.
DR PIR; F70048; F70048.
DR RefSeq; NP_391180.2; NC_000964.3.
DR RefSeq; WP_003228534.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; Q9R9I1; -.
DR SMR; Q9R9I1; -.
DR IntAct; Q9R9I1; 4.
DR STRING; 224308.BSU33000; -.
DR MEROPS; S01.B81; -.
DR PaxDb; Q9R9I1; -.
DR PRIDE; Q9R9I1; -.
DR EnsemblBacteria; CAB15290; CAB15290; BSU_33000.
DR GeneID; 935935; -.
DR KEGG; bsu:BSU33000; -.
DR PATRIC; fig|224308.179.peg.3576; -.
DR eggNOG; COG0265; Bacteria.
DR InParanoid; Q9R9I1; -.
DR OMA; SSYPEQD; -.
DR PhylomeDB; Q9R9I1; -.
DR BioCyc; BSUB:BSU33000-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR Pfam; PF13180; PDZ_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW Serine protease; Stress response; Transmembrane; Transmembrane helix.
FT CHAIN 1..458
FT /note="Serine protease Do-like HtrB"
FT /id="PRO_0000093867"
FT TOPO_DOM 1..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..458
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 356..440
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 187
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 217
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 298
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT BINDING 296..298
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 352..356
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 458 AA; 48717 MW; 77551045A865A5CD CRC64;
MDYRRDGQND QHQTEPSHTE QQNTENQKLI GHSEQELLDA PVSYEAGRQE TASALEMEKQ
ETAVKKEKKR RAAWLSPILG GIIGGGLMLG IAPYLPSDQN QATETASANK QVQSDNFTTA
PITNASNIAD MVEDLEPTIV GISNIQTSQN NTFGTGGGSS SESESGTGSG VIFKKDSDKA
YIITNNHVVE GANKLTVTLY NGETETAKLV GSDTITDLAV LEISGKNVKK VASFGDSSQL
RTGEKVIAIG NPLGQQFSGT VTQGIISGLN RTIDVDTTQG TVEMNVLQTD AAINPGNSGG
PLINASGQVI GINSLKVSES GVESLGFAIP SNDVEPIVDQ LLQNGKVDRP FLGVQMIDMS
QVPETYQENT LGLFGDQLGK GVYVKEVQAN SPAEKAGIKS EDVIVKLNGK DVESSADIRQ
ILYKDLKVGD KTTIQVLRKG KTKTLNATLT KQTESSSS
