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Database: UniProt
Entry: A0A024Q9R0_9BACI
LinkDB: A0A024Q9R0_9BACI
Original site: A0A024Q9R0_9BACI 
ID   A0A024Q9R0_9BACI        Unreviewed;      1440 AA.
AC   A0A024Q9R0;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Bacillopeptidase F {ECO:0000313|EMBL:CDQ39234.1};
DE   Flags: Precursor;
GN   Name=bpr_2 {ECO:0000313|EMBL:CDQ39234.1};
GN   ORFNames=BN990_01520 {ECO:0000313|EMBL:CDQ39234.1};
OS   Virgibacillus massiliensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=1462526 {ECO:0000313|EMBL:CDQ39234.1, ECO:0000313|Proteomes:UP000028875};
RN   [1] {ECO:0000313|EMBL:CDQ39234.1, ECO:0000313|Proteomes:UP000028875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Vm-5 {ECO:0000313|EMBL:CDQ39234.1,
RC   ECO:0000313|Proteomes:UP000028875};
RA   Urmite Genomes U.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000028875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Vm-5 {ECO:0000313|Proteomes:UP000028875};
RA   Khelaifia S., Croce O., Lagier J.C., Raoult D.;
RT   "Draft genome sequence of Virgibacillus massiliensis Vm-5.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDQ39234.1}.
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DR   EMBL; CCDP010000001; CDQ39234.1; -; Genomic_DNA.
DR   STRING; 1462526.BN990_01520; -.
DR   eggNOG; COG1404; Bacteria.
DR   eggNOG; COG4412; Bacteria.
DR   OrthoDB; 9798386at2; -.
DR   Proteomes; UP000028875; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07481; Peptidases_S8_BacillopeptidaseF-like; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR033857; Bacillopeptidase_F.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR012103; Pept_S8A_Bpr.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   NCBIfam; NF038128; choice_anch_J; 1.
DR   PANTHER; PTHR43399:SF5; CELL WALL-ASSOCIATED PROTEASE; 1.
DR   PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR   Pfam; PF13620; CarboxypepD_reg; 1.
DR   Pfam; PF09136; Glucodextran_B; 1.
DR   Pfam; PF20773; InhA-like_MAM; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PIRSF; PIRSF015477; Bpr; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000028875};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..1440
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001532800"
FT   DOMAIN          69..177
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          215..496
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        224
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015477-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        270
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015477-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        444
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015477-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1440 AA;  154463 MW;  C8F36C2AF0F8A244 CRC64;
     MKAKRRRQSK ALSVAATVLM TFSLITPGLA NAESSGKLHQ AARDSNKTVE EKVSDRLVKE
     FKDDEKVTFL VKFSEKADVT KVAENAKSDA AKASLSAQKA EHVQRSAVIS ELKTTALESQ
     ENVKAFLEEQ ESKGNVEKFK SYHIVNGMAV TATKKVAEKI ASFAEVEKIL PNEERELYDV
     TIDKEAGEVA SELANIEWNV ERVGAPSVWE MGFDGTGTVV ASIDSGAQWD HPALQEKYRG
     YNAETGEVDH TYSFFDATAD EEEAYDDHGH GTHVTGTMVG SEPDGSNQIG VAPGAKWISA
     KGLNAAGSGY DTWLLAAAEW MLAPGGDASM APDVVNNSWG GGPGLDEWYR DVVTAWRAAE
     IFPEFSAGNT TLTNPGGPGS VAVPANYPES FATGATDSED LLASFSLQGP SPYDEIKPEI
     SAPGVNIRSS VPGGGYEGGW NGTSMAGPAV SAVVALMKQA DASLTVDELE EILMTTANPL
     TDDEFPESPN NGYGAGLVNA YDAVSSLVTG LGTIEGQVTK AGEDAEAPTF EHEGITESYI
     GMDLDLTIEV TDNISVNNVT LEYTNQDGET QSVEAERISG DYKQGEYQAT IPGEQLTGES
     LSYNWVINDF GDNEVTSDSY EVALLPGVSV GFSDDFESPS AGWSVIGEGN SWERGVPTSG
     PESAASGENV YATNLAGEYD NNANTTLVMP PIDLPEGEAY LQFNQWYNIE NNWDYGHVFI
     STDQEEWTQL LRVTDTTDGW ENAEVDLSEY SGQRVYIGFN LDSDGSVSRE GWYIDDVTLA
     ETSNSESASV SKDKGYVGVV GFDNALSIVK NDKKASLKEE VNPAKIQPVN PKKELDPEKD
     TISPALLPMS AQVSVLESGR SVATDPATGG YTLLHAAGDF TVKAEAYGFE SQEQAVTVEA
     DGTTEADFTL EEMDQFTVSG TVTDQQTGEP VSGATLLLEE DANVEPVTTD EEGNYSLTAY
     KGSYTLKVVA SGYHGTEVEV SLEDGDVTEN VELEPFYTVP GGEIAYDDGT AENARAFYDA
     FNGWGVKMTL PEGEESGVVD AAVFKFWDEE FPNPGGTEFQ VEIWDATGTD GAPGEKLAGP
     FDAEAIRDSN EWTVIDLSEH GIVVDKEFYV VYVQTATNTE APGLATDESS QNAERSYQLV
     GGTWSKSPSA EGNYMIRARV NYEVEEPVIT APANDTITNE TEVTVEGTAS PTTTIQLLNN
     GEEVGTAEIG EDGAFAIPTT LSEGANELTA VSLLDGTPTG ESEPVNVTLD TESPELTIDN
     PEDGEKSNRE TVTVEGTVSD TNLDVVEVNG QEADVEEGSY SKRILLDEGE NQIEVVAHDL
     AGNTATESVT LDVDFTAPEI ENLTPEEDVN LEAGQTVKFE FDSEPGLKAS YFIHMPLTNT
     VTNATELPMM ETSEGHYVGY WTATSNVVAE GAVIEVKVED DYGNETREQA EGKLYINVAE
//
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