HTRA_BACSU
ID HTRA_BACSU Reviewed; 449 AA.
AC O34358;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Serine protease Do-like HtrA;
DE EC=3.4.21.107;
DE AltName: Full=HtrA-like serine protease;
GN Name=htrA; Synonyms=ykdA; OrderedLocusNames=BSU12900;
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;
RA Devine K.M.;
RT "Sequence of the Bacillus subtilis genome between xlyA and ykoR.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP SEQUENCE REVISION TO 72.
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 [4]
RP INDUCTION.
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 [5]
RP INDUCTION, DISRUPTION PHENOTYPE, AND FUNCTION.
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).
RN [6]
RP INDUCTION.
RC STRAIN=168;
RX PubMed=11555295; DOI=10.1046/j.1365-2958.2001.02576.x;
RA Hyyrylaeinen H.-L., Bolhuis A., Darmon E., Muukkonen L., Koski P.,
RA Vitikainen M., Sarvas M., Pragai Z., Bron S., van Dijl J.M., Kontinen V.P.;
RT "A novel two-component regulatory system in Bacillus subtilis for the
RT survival of severe secretion stress.";
RL Mol. Microbiol. 41:1159-1172(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|PubMed:11133960}.
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: Transcription is CssS dependent. Induced by heat shock
CC during exponential growth and by heterologous amylases at the
CC transition phase of the growth cycle. Negatively regulates its own
CC expression during exponential growth and during heat shock.
CC {ECO:0000269|PubMed:10692364, ECO:0000269|PubMed:11133960,
CC ECO:0000269|PubMed:11555295}.
CC -!- DISRUPTION PHENOTYPE: In contrast to other bacteria, in which
CC inactivation of serine protease leads to thermosensitivity,
CC inactivation of HtrA 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 YtvA, especially during stress conditions.
CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR EMBL; AJ002571; CAA05570.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13147.2; -; Genomic_DNA.
DR PIR; A69643; A69643.
DR RefSeq; NP_389173.2; NC_000964.3.
DR RefSeq; WP_009967069.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O34358; -.
DR SMR; O34358; -.
DR IntAct; O34358; 3.
DR STRING; 224308.BSU12900; -.
DR MEROPS; S01.B81; -.
DR PaxDb; O34358; -.
DR PRIDE; O34358; -.
DR EnsemblBacteria; CAB13147; CAB13147; BSU_12900.
DR GeneID; 939849; -.
DR KEGG; bsu:BSU12900; -.
DR PATRIC; fig|224308.179.peg.1402; -.
DR eggNOG; COG0265; Bacteria.
DR InParanoid; O34358; -.
DR OMA; THGWVLE; -.
DR PhylomeDB; O34358; -.
DR BioCyc; BSUB:BSU12900-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..449
FT /note="Serine protease Do-like HtrA"
FT /id="PRO_0000093859"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..449
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 348..437
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 179
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 209
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 290
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT BINDING 288..290
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 344..348
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 72
FT /note="D -> N (in Ref. 1; CAA05570)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 449 AA; 47715 MW; 8E4A28CDE18C4612 CRC64;
MDNYRDENRT KGNENEVFLT KENDQSASYS ARNVIHDQEK KKRGFGWFRP LLGGVIGGSL
ALGIYTFTPL GDHDSQDTAK QSSSQQQTQS VTATSTSSES KKSSSSSSAF KSEDSSKISD
MVEDLSPAIV GITNLQAQSN SSLFGSSSSD SSEDTESGSG SGVIFKKENG KAYIITNNHV
VEGASSLKVS LYDGTEVTAK LVGSDSLTDL AVLQISDDHV TKVANFGDSS DLRTGETVIA
IGDPLGKDLS RTVTQGIVSG VDRTVSMSTS AGETSINVIQ TDAAINPGNS GGPLLNTDGK
IVGINSMKIS EDDVEGIGFA IPSNDVKPIA EELLSKGQIE RPYIGVSMLD LEQVPQNYQE
GTLGLFGSQL NKGVYIREVA SGSPAEKAGL KAEDIIIGLK GKEIDTGSEL RNILYKDAKI
GDTVEVKILR NGKEMTKKIK LDQKEEKTS
