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APRX_BACSU
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   03-AUG-2022, entry version 120.
DE   RecName: Full=Serine protease AprX;
DE            EC=3.4.21.-;
GN   Name=aprX; OrderedLocusNames=BSU17260;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; 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; O31788; -.
DR   PRIDE; O31788; -.
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   OMA; FNKINCC; -.
DR   PhylomeDB; O31788; -.
DR   BioCyc; BSUB:BSU17260-MON; -.
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   Gene3D; 3.40.50.200; -; 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   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; SSF52743; 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
 
 
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