ID APRX_BACSU Reviewed; 442 AA.
AC O31788;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE RecName: Full=Serine protease AprX;
DE EC=3.4.21.-;
GN Name=aprX; OrderedLocusNames=BSU17260;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=10589719; DOI=10.1099/00221287-145-11-3121;
RA Valbuzzi A., Ferrari E., Albertini A.M.;
RT "A novel member of the subtilisin-like protease family from Bacillus
RT subtilis.";
RL Microbiology 145:3121-3127(1999).
RN [3]
RP FUNCTION AS A PROTEASE, ACTIVITY REGULATION, INDUCTION, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=168;
RX PubMed=17884659; DOI=10.1263/jbb.104.135;
RA Kodama T., Endo K., Sawada K., Ara K., Ozaki K., Kakeshita H., Yamane K.,
RA Sekiguchi J.;
RT "Bacillus subtilis AprX involved in degradation of a heterologous protein
RT during the late stationary growth phase.";
RL J. Biosci. Bioeng. 104:135-143(2007).
CC -!- FUNCTION: Displays serine protease activity. Seems to have a broad
CC substrate specificity. {ECO:0000269|PubMed:17884659}.
CC -!- ACTIVITY REGULATION: Is completely inhibited by
CC phenylmethanesulphonylfluoride (PMSF) in vitro.
CC {ECO:0000269|PubMed:17884659}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:17884659}. Note=Is
CC leaked to the culture medium during the late stationary phase owing to
CC cell lysis.
CC -!- INDUCTION: Is expressed during the late stationary phase of growth. Is
CC down-regulated by SinR. {ECO:0000269|PubMed:10589719,
CC ECO:0000269|PubMed:17884659}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show normal growth and
CC sporulation. {ECO:0000269|PubMed:10589719}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AL009126; CAB13610.1; -; Genomic_DNA.
DR PIR; A69587; A69587.
DR RefSeq; NP_389608.1; NC_000964.3.
DR RefSeq; WP_009967303.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O31788; -.
DR SMR; O31788; -.
DR STRING; 224308.BSU17260; -.
DR MEROPS; S08.137; -.
DR PaxDb; 224308-BSU17260; -.
DR EnsemblBacteria; CAB13610; CAB13610; BSU_17260.
DR GeneID; 940056; -.
DR KEGG; bsu:BSU17260; -.
DR PATRIC; fig|224308.179.peg.1871; -.
DR eggNOG; COG1404; Bacteria.
DR InParanoid; O31788; -.
DR OrthoDB; 9798386at2; -.
DR PhylomeDB; O31788; -.
DR BioCyc; BSUB:BSU17260-MONOMER; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07487; Peptidases_S8_1; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Protease; Reference proteome; Serine protease.
FT CHAIN 1..442
FT /note="Serine protease AprX"
FT /id="PRO_0000390778"
FT DOMAIN 122..439
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 318..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 155
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 187
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 384
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 442 AA; 47906 MW; B996446AE87BADF2 CRC64;
MFGYSMVQMV RANAHKLDWP LRETVLQLYK PFKWTPCFLH KFFETKLQNR KKMSVIIEFE
EGCHETGFQM AGEVLQKEKR SKLKSRFNKI NCCSAEVTPS ALHSLLSECS NIRKVYLNRE
VKALLDTATE ASHAKEVVRN GQTLTGKGVT VAVVDTGIYP HPDLEGRIIG FADMVNQKTE
PYDDNGHGTH CAGDVASSGA SSSGQYRGPA PEANLIGVKV LNKQGSGTLA DIIEGVEWCI
QYNEDNPDEP IDIMSMSLGG DALRYDHEQE DPLVRAVEEA WSAGIVVCVA AGNSGPDSQT
IASPGVSEKV ITVGALDDNN TASSDDDTVA SFSSRGPTVY GKEKPDILAP GVNIISLRSP
NSYIDKLQKS SRVGSQYFTM SGTSMATPIC AGIAALILQQ NPDLTPDEVK ELLKNGTDKW
KDEDPNIYGA GAVNAENSVP GQ
//
