SUBV_BACSU
ID SUBV_BACSU Reviewed; 806 AA.
AC P29141;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Minor extracellular protease vpr;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=vpr; OrderedLocusNames=BSU38090; ORFNames=ipa-45r;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 161-195.
RX PubMed=1938892; DOI=10.1128/jb.173.21.6889-6895.1991;
RA Sloma A., Rufo G.A. Jr., Theriault K.A., Dwyer M., Wilson S.W., Pero J.;
RT "Cloning and characterization of the gene for an additional extracellular
RT serine protease of Bacillus subtilis.";
RL J. Bacteriol. 173:6889-6895(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
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 PROTEIN SEQUENCE OF 161-170.
RC STRAIN=168;
RX PubMed=10658653; DOI=10.1099/00221287-146-1-65;
RA Hirose I., Sano K., Shioda I., Kumano M., Nakamura K., Yamane K.;
RT "Proteome analysis of Bacillus subtilis extracellular proteins: a two-
RT dimensional protein electrophoretic study.";
RL Microbiology 146:65-75(2000).
CC -!- FUNCTION: Not required for growth or sporulation.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Probably undergoes C-terminal processing or proteolysis.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; M76590; AAA22881.1; -; Genomic_DNA.
DR EMBL; X73124; CAA51601.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15835.1; -; Genomic_DNA.
DR PIR; A41341; A41341.
DR RefSeq; NP_391688.1; NC_000964.3.
DR RefSeq; WP_003227419.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P29141; -.
DR SMR; P29141; -.
DR STRING; 224308.BSU38090; -.
DR MEROPS; S08.114; -.
DR PaxDb; P29141; -.
DR PRIDE; P29141; -.
DR EnsemblBacteria; CAB15835; CAB15835; BSU_38090.
DR GeneID; 937291; -.
DR KEGG; bsu:BSU38090; -.
DR PATRIC; fig|224308.179.peg.4123; -.
DR eggNOG; COG1404; Bacteria.
DR InParanoid; P29141; -.
DR OMA; FKWNGTK; -.
DR PhylomeDB; P29141; -.
DR BioCyc; BSUB:BSU38090-MON; -.
DR BRENDA; 3.4.21.62; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; 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; cd07474; Peptidases_S8_subtilisin_Vpr-like; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR025965; FlgD_Ig.
DR InterPro; IPR003137; PA_domain.
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 InterPro; IPR034213; S8_Vpr-like.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR Pfam; PF13860; FlgD_ig; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 1.
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 Direct protein sequencing; Hydrolase; Protease; Reference proteome;
KW Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..160
FT /evidence="ECO:0000269|PubMed:10658653,
FT ECO:0000269|PubMed:1938892"
FT /id="PRO_0000027189"
FT CHAIN 161..806
FT /note="Minor extracellular protease vpr"
FT /id="PRO_0000027190"
FT DOMAIN 57..142
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 158..597
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 189
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 233
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 534
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 806 AA; 85608 MW; F984E3BF0B869DDD CRC64;
MKKGIIRFLL VSFVLFFALS TGITGVQAAP ASSKTSADLE KAEVFGDIDM TTSKKTTVIV
ELKEKSLAEA KEAGESQSKS KLKTARTKAK NKAIKAVKNG KVNREYEQVF SGFSMKLPAN
EIPKLLAVKD VKAVYPNVTY KTDNMKDKDV TISEDAVSPQ MDDSAPYIGA NDAWDLGYTG
KGIKVAIIDT GVEYNHPDLK KNFGQYKGYD FVDNDYDPKE TPTGDPRGEA TDHGTHVAGT
VAANGTIKGV APDATLLAYR VLGPGGSGTT ENVIAGVERA VQDGADVMNL SLGNSLNNPD
WATSTALDWA MSEGVVAVTS NGNSGPNGWT VGSPGTSREA ISVGATQLPL NEYAVTFGSY
SSAKVMGYNK EDDVKALNNK EVELVEAGIG EAKDFEGKDL TGKVAVVKRG SIAFVDKADN
AKKAGAIGMV VYNNLSGEIE ANVPGMSVPT IKLSLEDGEK LVSALKAGET KTTFKLTVSK
ALGEQVADFS SRGPVMDTWM IKPDISAPGV NIVSTIPTHD PDHPYGYGSK QGTSMASPHI
AGAVAVIKQA KPKWSVEQIK AAIMNTAVTL KDSDGEVYPH NAQGAGSARI MNAIKADSLV
SPGSYSYGTF LKENGNETKN ETFTIENQSS IRKSYTLEYS FNGSGISTSG TSRVVIPAHQ
TGKATAKVKV NTKKTKAGTY EGTVIVREGG KTVAKVPTLL IVKEPDYPRV TSVSVSEGSV
QGTYQIETYL PAGAEELAFL VYDSNLDFAG QAGIYKNQDK GYQYFDWDGT INGGTKLPAG
EYYLLAYAAN KGKSSQVLTE EPFTVE